{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,23]],"date-time":"2026-04-23T15:48:50Z","timestamp":1776959330935,"version":"3.51.4"},"reference-count":52,"publisher":"Springer Science and Business Media LLC","issue":"4","license":[{"start":{"date-parts":[[2018,3,7]],"date-time":"2018-03-07T00:00:00Z","timestamp":1520380800000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/www.springer.com\/tdm"}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["J Comput Aided Mol Des"],"published-print":{"date-parts":[[2018,4]]},"DOI":"10.1007\/s10822-018-0109-y","type":"journal-article","created":{"date-parts":[[2018,3,7]],"date-time":"2018-03-07T03:45:11Z","timestamp":1520394311000},"page":"559-572","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":16,"title":["Insight into microtubule destabilization mechanism of 3,4,5-trimethoxyphenyl indanone derivatives using molecular dynamics simulation and conformational modes analysis"],"prefix":"10.1007","volume":"32","author":[{"given":"Shubhandra","family":"Tripathi","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Gaurava","family":"Srivastava","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Aastha","family":"Singh","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"A. P.","family":"Prakasham","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Arvind S.","family":"Negi","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4843-0248","authenticated-orcid":false,"given":"Ashok","family":"Sharma","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"297","published-online":{"date-parts":[[2018,3,7]]},"reference":[{"key":"109_CR1","doi-asserted-by":"publisher","first-page":"253","DOI":"10.1038\/nrc1317","volume":"4","author":"MA Jordan","year":"2004","unstructured":"Jordan MA, Wilson L (2004) Microtubules as a target for anticancer drugs. Nat Rev Cancer 4:253\u2013265. \n                    https:\/\/doi.org\/10.1038\/nrc1317","journal-title":"Nat Rev Cancer"},{"key":"109_CR2","doi-asserted-by":"publisher","first-page":"443","DOI":"10.1002\/med.20242","volume":"31","author":"RA Stanton","year":"2011","unstructured":"Stanton RA, Gernert KM, Nettles JH, Aneja R (2011) Drugs that target dynamic microtubules: a new molecular perspective. Med Res Rev 31:443\u2013481. \n                    https:\/\/doi.org\/10.1002\/med.20242","journal-title":"Med Res Rev"},{"key":"109_CR3","doi-asserted-by":"publisher","first-page":"237","DOI":"10.1038\/312237a0","volume":"312","author":"T Mitchison","year":"1984","unstructured":"Mitchison T, Kirschner M (1984) Dynamic instability of microtubule growth. Nature 312:237\u2013242. \n                    https:\/\/doi.org\/10.1038\/312237a0","journal-title":"Nature"},{"key":"109_CR4","doi-asserted-by":"publisher","first-page":"102","DOI":"10.1111\/febs.13555","volume":"283","author":"Y Wang","year":"2016","unstructured":"Wang Y, Zhang H, Gigant B et al (2016) Structures of a diverse set of colchicine binding site inhibitors in complex with tubulin provide a rationale for drug discovery. FEBS J 283:102\u2013111. \n                    https:\/\/doi.org\/10.1111\/febs.13555","journal-title":"FEBS J"},{"key":"109_CR5","doi-asserted-by":"publisher","first-page":"198","DOI":"10.1038\/nature02393","volume":"428","author":"RBG Ravelli","year":"2004","unstructured":"Ravelli RBG, Gigant B, Curmi PA et al (2004) Insight into tubulin regulation from a complex with colchicine and a stathmin-like domain. Nature 428:198\u2013202. \n                    https:\/\/doi.org\/10.1038\/nature02393","journal-title":"Nature"},{"key":"109_CR6","doi-asserted-by":"publisher","first-page":"13775","DOI":"10.1073\/pnas.0904223106","volume":"106","author":"A Dorleans","year":"2009","unstructured":"Dorleans A, Gigant B, Ravelli RBG et al (2009) Variations in the colchicine-binding domain provide insight into the structural switch of tubulin. Proc Natl Acad Sci 106:13775\u201313779. \n                    https:\/\/doi.org\/10.1073\/pnas.0904223106","journal-title":"Proc Natl Acad Sci"},{"key":"109_CR7","doi-asserted-by":"publisher","first-page":"7138","DOI":"10.1021\/bi300474q","volume":"51","author":"S Chakraborti","year":"2012","unstructured":"Chakraborti S, Chakravarty D, Gupta S et al (2012) Discrimination of ligands with different flexibilities resulting from the plasticity of the binding site in tubulin. Biochemistry 51:7138\u20137148. \n                    https:\/\/doi.org\/10.1021\/bi300474q","journal-title":"Biochemistry"},{"key":"109_CR8","doi-asserted-by":"publisher","first-page":"e0156048","DOI":"10.1371\/journal.pone.0156048","volume":"11","author":"BV Kumbhar","year":"2016","unstructured":"Kumbhar BV, Borogaon A, Panda D, Kunwar A (2016) Exploring the origin of differential binding affinities of human tubulin isotypes \u03b1\u03b2II, \u03b1\u03b2III and \u03b1\u03b2IV for DAMA-colchicine using homology modelling, molecular docking and molecular dynamics simulations. PLoS ONE 11:e0156048. \n                    https:\/\/doi.org\/10.1371\/journal.pone.0156048","journal-title":"PLoS ONE"},{"key":"109_CR9","doi-asserted-by":"publisher","first-page":"118","DOI":"10.1021\/acs.jpcb.6b11322","volume":"121","author":"S Majumdar","year":"2017","unstructured":"Majumdar S, Ghosh Dastidar S (2017) Ligand binding swaps between soft internal modes of \u03b1,\u03b2-tubulin and alters its accessible conformational space. J Phys Chem B 121:118\u2013128. \n                    https:\/\/doi.org\/10.1021\/acs.jpcb.6b11322","journal-title":"J Phys Chem B"},{"key":"109_CR10","doi-asserted-by":"publisher","first-page":"e1003464","DOI":"10.1371\/journal.pcbi.1003464","volume":"10","author":"LX Peng","year":"2014","unstructured":"Peng LX, Hsu MT, Bonomi M et al (2014) The free energy profile of tubulin straight-bent conformational changes, with implications for microtubule assembly and drug discovery. PLoS Comput Biol 10:e1003464. \n                    https:\/\/doi.org\/10.1371\/journal.pcbi.1003464","journal-title":"PLoS Comput Biol"},{"key":"109_CR11","doi-asserted-by":"publisher","first-page":"335","DOI":"10.1021\/acs.biochem.5b00853","volume":"55","author":"S Majumdar","year":"2016","unstructured":"Majumdar S, Maiti S, Ghosh Dastidar S (2016) Dynamic and static water molecules complement the TN16 conformational heterogeneity inside the tubulin cavity. Biochemistry 55:335\u2013347. \n                    https:\/\/doi.org\/10.1021\/acs.biochem.5b00853","journal-title":"Biochemistry"},{"key":"109_CR12","doi-asserted-by":"publisher","first-page":"2487","DOI":"10.1529\/biophysj.108.129072","volume":"95","author":"Y Gebremichael","year":"2008","unstructured":"Gebremichael Y, Chu J-W, Voth GA (2008) Intrinsic bending and structural rearrangement of tubulin dimer: molecular dynamics simulations and coarse-grained analysis. Biophys J 95:2487\u20132499. \n                    https:\/\/doi.org\/10.1529\/biophysj.108.129072","journal-title":"Biophys J"},{"key":"109_CR13","doi-asserted-by":"publisher","first-page":"663","DOI":"10.1016\/S0006-3495(02)75199-0","volume":"83","author":"O Keskin","year":"2002","unstructured":"Keskin O, Durell SR, Bahar I et al (2002) Relating molecular flexibility to function: a case study of tubulin. Biophys J 83:663\u2013680. \n                    https:\/\/doi.org\/10.1016\/S0006-3495(02)75199-0","journal-title":"Biophys J"},{"key":"109_CR14","doi-asserted-by":"publisher","first-page":"256","DOI":"10.1016\/S0959-440X(03)00029-0","volume":"13","author":"E Nogales","year":"2003","unstructured":"Nogales E (2003) Tubulin rings: which way do they curve?. Curr Opin Struct Biol 13:256\u2013261. \n                    https:\/\/doi.org\/10.1016\/S0959-440X(03)00029-0","journal-title":"Curr Opin Struct Biol"},{"key":"109_CR15","doi-asserted-by":"publisher","first-page":"3914","DOI":"10.1016\/j.bmcl.2008.06.039","volume":"18","author":"HO Saxena","year":"2008","unstructured":"Saxena HO, Faridi U, Srivastava S et al (2008) Gallic acid-based indanone derivatives as anticancer agents. Bioorg Med Chem Lett 18:3914\u20133918. \n                    https:\/\/doi.org\/10.1016\/j.bmcl.2008.06.039","journal-title":"Bioorg Med Chem Lett"},{"key":"109_CR16","doi-asserted-by":"publisher","first-page":"3049","DOI":"10.1016\/j.bmc.2012.02.057","volume":"20","author":"AP Prakasham","year":"2012","unstructured":"Prakasham AP, Saxena AK, Luqman S et al (2012) Synthesis and anticancer activity of 2-benzylidene indanones through inhibiting tubulin polymerization. Bioorg Med Chem 20:3049\u20133057. \n                    https:\/\/doi.org\/10.1016\/j.bmc.2012.02.057","journal-title":"Bioorg Med Chem"},{"key":"109_CR17","doi-asserted-by":"publisher","first-page":"373","DOI":"10.1016\/j.bmc.2014.12.027","volume":"23","author":"AS Negi","year":"2015","unstructured":"Negi AS, Gautam Y, Alam S et al (2015) Natural antitubulin agents: Importance of 3,4,5-trimethoxyphenyl fragment. Bioorg Med Chem 23:373\u2013389. \n                    https:\/\/doi.org\/10.1016\/j.bmc.2014.12.027","journal-title":"Bioorg Med Chem"},{"key":"109_CR18","doi-asserted-by":"publisher","first-page":"625","DOI":"10.1111\/cbdd.12805","volume":"88","author":"A Singh","year":"2016","unstructured":"Singh A, Fatima K, Srivastava A et al (2016) Anticancer activity of gallic acid template-based benzylidene indanone derivative as microtubule destabilizer. Chem Biol Drug Des 88:625\u2013634. \n                    https:\/\/doi.org\/10.1111\/cbdd.12805","journal-title":"Chem Biol Drug Des"},{"key":"109_CR19","doi-asserted-by":"publisher","first-page":"988","DOI":"10.1016\/j.ejps.2012.08.013","volume":"47","author":"D Chanda","year":"2012","unstructured":"Chanda D, Bhushan S, Guru SK et al (2012) Anticancer activity, toxicity and pharmacokinetic profile of an indanone derivative. Eur J Pharm Sci 47:988\u2013995. \n                    https:\/\/doi.org\/10.1016\/j.ejps.2012.08.013","journal-title":"Eur J Pharm Sci"},{"key":"109_CR20","doi-asserted-by":"publisher","first-page":"3033","DOI":"10.1021\/jm0512903","volume":"49","author":"GC Tron","year":"2006","unstructured":"Tron GC, Pirali T, Sorba G et al (2006) Medicinal chemistry of combretastatin A4: present and future directions. J Med Chem 49:3033\u20133044. \n                    https:\/\/doi.org\/10.1021\/jm0512903","journal-title":"J Med Chem"},{"key":"109_CR21","doi-asserted-by":"publisher","first-page":"234","DOI":"10.1016\/j.bmc.2011.11.010","volume":"20","author":"\u00d8W Akselsen","year":"2012","unstructured":"Akselsen \u00d8W, Odlo K, Cheng J-J et al (2012) Synthesis, biological evaluation and molecular modeling of 1,2,3-triazole analogs of combretastatin A-1. Bioorg Med Chem 20:234\u2013242. \n                    https:\/\/doi.org\/10.1016\/j.bmc.2011.11.010","journal-title":"Bioorg Med Chem"},{"key":"109_CR22","doi-asserted-by":"publisher","first-page":"766","DOI":"10.1039\/C3MD00357D","volume":"5","author":"N Sanghai","year":"2014","unstructured":"Sanghai N, Jain V, Preet R et al (2014) Combretastatin A-4 inspired novel 2-aryl-3-arylamino-imidazo-pyridines\/pyrazines as tubulin polymerization inhibitors, antimitotic and anticancer agents. Med Chem Commun 5:766\u2013782. \n                    https:\/\/doi.org\/10.1039\/C3MD00357D","journal-title":"Med Chem Commun"},{"key":"109_CR23","doi-asserted-by":"publisher","first-page":"273","DOI":"10.1016\/j.bbrc.2016.05.112","volume":"476","author":"S Tripathi","year":"2016","unstructured":"Tripathi S, Srivastava G, Sharma A (2016) Molecular dynamics simulation and free energy landscape methods in probing L215H, L217R and L225M \u03b2I-tubulin mutations causing paclitaxel resistance in cancer cells. Biochem Biophys Res Commun 476:273\u2013279. \n                    https:\/\/doi.org\/10.1016\/j.bbrc.2016.05.112","journal-title":"Biochem Biophys Res Commun"},{"key":"109_CR24","doi-asserted-by":"publisher","first-page":"18","DOI":"10.1016\/j.tube.2017.04.002","volume":"105","author":"G Srivastava","year":"2017","unstructured":"Srivastava G, Tripathi S, Kumar A, Sharma A (2017) Molecular investigation of active binding site of isoniazid (INH) and insight into resistance mechanism of S315T-MtKatG in Mycobacterium tuberculosis. Tuberculosis 105:18\u201327. \n                    https:\/\/doi.org\/10.1016\/j.tube.2017.04.002","journal-title":"Tuberculosis"},{"key":"109_CR25","doi-asserted-by":"publisher","first-page":"392","DOI":"10.1021\/jp5079554","volume":"119","author":"B Singh","year":"2015","unstructured":"Singh B, Bulusu G, Mitra A (2015) Understanding the thermostability and activity of Bacillus subtilis lipase mutants: insights from molecular dynamics simulations. J Phys Chem B 119:392\u2013409. \n                    https:\/\/doi.org\/10.1021\/jp5079554","journal-title":"J Phys Chem B"},{"key":"109_CR26","doi-asserted-by":"publisher","first-page":"899","DOI":"10.1007\/s10822-016-9978-0","volume":"30","author":"B Singh","year":"2016","unstructured":"Singh B, Bulusu G, Mitra A (2016) Effects of point mutations on the thermostability of B. subtilis lipase: investigating nonadditivity. J Comput Aided Mol Des 30:899\u2013916. \n                    https:\/\/doi.org\/10.1007\/s10822-016-9978-0","journal-title":"J Comput Aided Mol Des"},{"key":"109_CR27","doi-asserted-by":"publisher","DOI":"10.1002\/0471140864.ps0209s50","author":"N Eswar","year":"2007","unstructured":"Eswar N, Webb B, Marti-Renom MA et al (2007) Comparative protein structure modeling using MODELLER. Curr Protoc Protein Sci. \n                    https:\/\/doi.org\/10.1002\/0471140864.ps0209s50","journal-title":"Curr Protoc Protein Sci"},{"key":"109_CR28","doi-asserted-by":"publisher","first-page":"17","DOI":"10.1186\/1758-2946-4-17","volume":"4","author":"MD Hanwell","year":"2012","unstructured":"Hanwell MD, Curtis DE, Lonie DC et al (2012) Avogadro: an advanced semantic chemical editor, visualization, and analysis platform. J Cheminform 4:17. \n                    https:\/\/doi.org\/10.1186\/1758-2946-4-17","journal-title":"J Cheminform"},{"key":"109_CR29","doi-asserted-by":"publisher","first-page":"2785","DOI":"10.1002\/jcc.21256","volume":"30","author":"GM Morris","year":"2009","unstructured":"Morris GM, Huey R, Lindstrom W et al (2009) AutoDock4 and AutoDockTools4: automated docking with selective receptor flexibility. J Comput Chem 30:2785\u20132791. \n                    https:\/\/doi.org\/10.1002\/jcc.21256","journal-title":"J Comput Chem"},{"key":"109_CR30","doi-asserted-by":"publisher","first-page":"1639","DOI":"10.1002\/(SICI)1096-987X(19981115)19:14<1639::AID-JCC10>3.0.CO;2-B","volume":"19","author":"GM Morris","year":"1998","unstructured":"Morris GM, Goodsell DS, Halliday RS et al (1998) Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function. J Comput Chem 19:1639\u20131662","journal-title":"J Comput Chem"},{"key":"109_CR31","doi-asserted-by":"publisher","first-page":"1701","DOI":"10.1002\/jcc.20291","volume":"26","author":"D Spoel Van Der","year":"2005","unstructured":"Van Der Spoel D, Lindahl E, Hess B et al (2005) GROMACS: fast, flexible, and free. J Comput Chem 26:1701\u20131718. \n                    https:\/\/doi.org\/10.1002\/jcc.20291","journal-title":"J Comput Chem"},{"key":"109_CR32","doi-asserted-by":"publisher","first-page":"435","DOI":"10.1021\/ct700301q","volume":"4","author":"B Hess","year":"2008","unstructured":"Hess B, Kutzner C, van der Spoel D, Lindahl E (2008) GROMACS 4: algorithms for highly efficient, load-balanced, and scalable molecular simulation. J Chem Theory Comput 4:435\u2013447. \n                    https:\/\/doi.org\/10.1021\/ct700301q","journal-title":"J Chem Theory Comput"},{"key":"109_CR33","doi-asserted-by":"publisher","first-page":"1950","DOI":"10.1002\/prot.22711","volume":"78","author":"K Lindorff-Larsen","year":"2010","unstructured":"Lindorff-Larsen K, Piana S, Palmo K et al (2010) Improved side-chain torsion potentials for the Amber ff99SB protein force field. Proteins 78:1950\u20131958. \n                    https:\/\/doi.org\/10.1002\/prot.22711","journal-title":"Proteins"},{"key":"109_CR34","doi-asserted-by":"publisher","first-page":"1157","DOI":"10.1002\/jcc.20035","volume":"25","author":"J Wang","year":"2004","unstructured":"Wang J, Wolf RM, Caldwell JW et al (2004) Development and testing of a general amber force field. J Comput Chem 25:1157\u20131174. \n                    https:\/\/doi.org\/10.1002\/jcc.20035","journal-title":"J Comput Chem"},{"key":"109_CR35","doi-asserted-by":"publisher","first-page":"367","DOI":"10.1186\/1756-0500-5-367","volume":"5","author":"AW Sousa da Silva","year":"2012","unstructured":"Sousa da Silva AW, Vranken WF (2012) ACPYPE\u2014antechamber python parser interface. BMC Res Notes 5:367. \n                    https:\/\/doi.org\/10.1186\/1756-0500-5-367","journal-title":"BMC Res Notes"},{"key":"109_CR36","doi-asserted-by":"publisher","first-page":"1016","DOI":"10.1002\/jcc.10262","volume":"24","author":"KL Meagher","year":"2003","unstructured":"Meagher KL, Redman LT, Carlson HA (2003) Development of polyphosphate parameters for use with the AMBER force field. J Comput Chem 24:1016\u20131025. \n                    https:\/\/doi.org\/10.1002\/jcc.10262","journal-title":"J Comput Chem"},{"key":"109_CR37","doi-asserted-by":"publisher","first-page":"1493","DOI":"10.1021\/ct3000734","volume":"8","author":"O Alln\u00e9r","year":"2012","unstructured":"Alln\u00e9r O, Nilsson L, Villa A (2012) Magnesium ion\u2013water coordination and exchange in biomolecular simulations. J Chem Theory Comput 8:1493\u20131502. \n                    https:\/\/doi.org\/10.1021\/ct3000734","journal-title":"J Chem Theory Comput"},{"key":"109_CR38","doi-asserted-by":"publisher","first-page":"9954","DOI":"10.1021\/jp003020w","volume":"105","author":"P Mark","year":"2001","unstructured":"Mark P, Nilsson L (2001) Structure and dynamics of the TIP3P, SPC, and SPC\/E water models at 298\u00a0K. J Phys Chem A 105:9954\u20139960. \n                    https:\/\/doi.org\/10.1021\/jp003020w","journal-title":"J Phys Chem A"},{"key":"109_CR39","doi-asserted-by":"publisher","first-page":"014101","DOI":"10.1063\/1.2408420","volume":"126","author":"G Bussi","year":"2007","unstructured":"Bussi G, Donadio D, Parrinello M (2007) Canonical sampling through velocity rescaling. J Chem Phys 126:014101. \n                    https:\/\/doi.org\/10.1063\/1.2408420","journal-title":"J Chem Phys"},{"key":"109_CR40","doi-asserted-by":"publisher","first-page":"7182","DOI":"10.1063\/1.328693","volume":"52","author":"M Parrinello","year":"1981","unstructured":"Parrinello M (1981) Polymorphic transitions in single crystals: a new molecular dynamics method. J Appl Phys 52:7182. \n                    https:\/\/doi.org\/10.1063\/1.328693","journal-title":"J Appl Phys"},{"key":"109_CR41","doi-asserted-by":"publisher","first-page":"1463","DOI":"10.1002\/(SICI)1096-987X(199709)18:12<1463::AID-JCC4>3.0.CO;2-H","volume":"18","author":"B Hess","year":"1997","unstructured":"Hess B, Bekker H, Berendsen HJC, Fraaije JGEM (1997) LINCS: a linear constraint solver for molecular simulations. J Comput Chem 18:1463\u20131472.","journal-title":"J Comput Chem"},{"key":"109_CR42","doi-asserted-by":"publisher","first-page":"10089","DOI":"10.1063\/1.464397","volume":"98","author":"T Darden","year":"1993","unstructured":"Darden T, York D, Pedersen L (1993) Particle mesh Ewald: An N\u22c5log(N) method for Ewald sums in large systems. J Chem Phys 98:10089. \n                    https:\/\/doi.org\/10.1063\/1.464397","journal-title":"J Chem Phys"},{"key":"109_CR43","doi-asserted-by":"publisher","first-page":"2641","DOI":"10.1016\/j.cpc.2013.06.003","volume":"184","author":"S P\u00e1ll","year":"2013","unstructured":"P\u00e1ll S, Hess B (2013) A flexible algorithm for calculating pair interactions on SIMD architectures. Comput Phys Commun 184:2641\u20132650. \n                    https:\/\/doi.org\/10.1016\/j.cpc.2013.06.003","journal-title":"Comput Phys Commun"},{"key":"109_CR44","doi-asserted-by":"publisher","first-page":"33","DOI":"10.1016\/0263-7855(96)00018-5","volume":"14","author":"W Humphrey","year":"1996","unstructured":"Humphrey W, Dalke A, Schulten K (1996) VMD: visual molecular dynamics. J Mol Graph 14:33\u201338","journal-title":"J Mol Graph"},{"key":"109_CR45","volume-title":"The Pymol molecular graphics system, version 0.99","author":"W DeLano","year":"2002","unstructured":"DeLano W (2002) The Pymol molecular graphics system, version 0.99. DeLano Scientific, San Carlos, CA"},{"key":"109_CR46","doi-asserted-by":"publisher","first-page":"2778","DOI":"10.1021\/ci200227u","volume":"51","author":"RA Laskowski","year":"2011","unstructured":"Laskowski RA, Swindells MB (2011) LigPlot+: multiple ligand\u2013protein interaction diagrams for drug discovery. J Chem Inf Model 51:2778\u20132786. \n                    https:\/\/doi.org\/10.1021\/ci200227u","journal-title":"J Chem Inf Model"},{"key":"109_CR47","unstructured":"http:\/\/plasma-gate.weizmann.ac.il\/Grace\/"},{"key":"109_CR48","doi-asserted-by":"publisher","first-page":"412","DOI":"10.1002\/prot.340170408","volume":"17","author":"A Amadei","year":"1993","unstructured":"Amadei A, Linssen AB, Berendsen HJ (1993) Essential dynamics of proteins. Proteins 17:412\u2013425. \n                    https:\/\/doi.org\/10.1002\/prot.340170408","journal-title":"Proteins"},{"key":"109_CR49","doi-asserted-by":"publisher","first-page":"1598","DOI":"10.1126\/science.1749933","volume":"254","author":"H Frauenfelder","year":"1991","unstructured":"Frauenfelder H, Sligar SG, Wolynes PG (1991) The energy landscapes and motions of proteins. Science 254:1598\u20131603","journal-title":"Science"},{"key":"109_CR50","doi-asserted-by":"publisher","first-page":"208106","DOI":"10.1103\/PhysRevLett.91.208106","volume":"91","author":"AL Tournier","year":"2003","unstructured":"Tournier AL, Smith JC (2003) Principal components of the protein dynamical transition. Phys Rev Lett 91:208106. \n                    https:\/\/doi.org\/10.1103\/PhysRevLett.91.208106","journal-title":"Phys Rev Lett"},{"key":"109_CR51","doi-asserted-by":"publisher","first-page":"1951","DOI":"10.1021\/ci500020m","volume":"54","author":"R Kumari","year":"2014","unstructured":"Kumari R, Kumar R, Open Source Drug Discovery Consortium, Lynn A (2014) g_mmpbsa A GROMACS tool for high-throughput MM-PBSA calculations. J Chem Inf Model 54:1951\u20131962. \n                    https:\/\/doi.org\/10.1021\/ci500020m","journal-title":"J Chem Inf Model"},{"key":"109_CR52","doi-asserted-by":"publisher","first-page":"2897","DOI":"10.1074\/jbc.271.6.2897","volume":"271","author":"G Chakrabarti","year":"1996","unstructured":"Chakrabarti G, Sengupta S, Bhattacharyya B (1996) Thermodynamics of colchicinoid-tubulin interactions role of B-ring and C-7 substituent. J Biol Chem 271:2897\u20132901","journal-title":"J Biol Chem"}],"container-title":["Journal of Computer-Aided Molecular Design"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/link.springer.com\/content\/pdf\/10.1007\/s10822-018-0109-y.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/link.springer.com\/article\/10.1007\/s10822-018-0109-y\/fulltext.html","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/link.springer.com\/content\/pdf\/10.1007\/s10822-018-0109-y.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2019,3,6]],"date-time":"2019-03-06T20:16:56Z","timestamp":1551903416000},"score":1,"resource":{"primary":{"URL":"http:\/\/link.springer.com\/10.1007\/s10822-018-0109-y"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2018,3,7]]},"references-count":52,"journal-issue":{"issue":"4","published-print":{"date-parts":[[2018,4]]}},"alternative-id":["109"],"URL":"https:\/\/doi.org\/10.1007\/s10822-018-0109-y","relation":{},"ISSN":["0920-654X","1573-4951"],"issn-type":[{"value":"0920-654X","type":"print"},{"value":"1573-4951","type":"electronic"}],"subject":[],"published":{"date-parts":[[2018,3,7]]},"assertion":[{"value":"24 October 2017","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"1 March 2018","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"7 March 2018","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Compliance with ethical standards"}},{"value":"The authors declare that they have no conflict of interest.","order":2,"name":"Ethics","group":{"name":"EthicsHeading","label":"<!--Emphasis Type='Bold' removed-->Conflict of interest"}}]}}