{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,7]],"date-time":"2026-03-07T01:39:29Z","timestamp":1772847569143,"version":"3.50.1"},"reference-count":67,"publisher":"Oxford University Press (OUP)","issue":"9","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2009,5,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:p>Motivation: Computational studies of the energetics of protein association are important for revealing the underlying fundamental principles and for designing better tools to model protein complexes. The interaction cutoff contribution to the ruggedness of protein\u2013protein energy landscape is studied in terms of relative energy fluctuations for 1\/rn potentials based on a simplistic model of a protein complex. This artificial ruggedness exists for short cutoffs and gradually disappears with the cutoff increase.<\/jats:p>\n               <jats:p>Results: The critical values of the cutoff were calculated for each of 11 popular power-type potentials with n=0\u00f79, 12 and for two thresholds of 5% and 10%. The artificial ruggedness decreases to tolerable thresholds for cutoffs larger than the critical ones. The results showed that for both thresholds the critical cutoff is a non-monotonic function of the potential power n. The functions reach the maximum at n=3\u00f74 and then decrease with the increase of the potential power. The difference between two cutoffs for 5% and 10% artificial ruggedness becomes negligible for potentials decreasing faster than 1\/r12. The analytical results obtained for the simple model of protein complexes agree with the analysis of artificial ruggedness in a dataset of 62 protein\u2013protein complexes, with different parameterizations of soft Lennard\u2013Jones potential and two types of protein representations: all-atom and coarse-grained. The results suggest that cutoffs larger than the critical ones can be recommended for protein\u2013protein potentials.<\/jats:p>\n               <jats:p>Contact: \u00a0vakser@ku.edu<\/jats:p>","DOI":"10.1093\/bioinformatics\/btp108","type":"journal-article","created":{"date-parts":[[2009,2,24]],"date-time":"2009-02-24T01:26:06Z","timestamp":1235438766000},"page":"1132-1136","source":"Crossref","is-referenced-by-count":4,"title":["The ruggedness of protein\u2013protein energy landscape and the cutoff for 1\/<i>r<\/i>\n                  <i>n<\/i> potentials"],"prefix":"10.1093","volume":"25","author":[{"given":"Anatoly M.","family":"Ruvinsky","sequence":"first","affiliation":[{"name":"1 Center for Bioinformatics and 2Department of Molecular Biosciences, The University of Kansas, Lawrence, KS 66047, USA"}]},{"given":"Ilya A.","family":"Vakser","sequence":"additional","affiliation":[{"name":"1 Center for Bioinformatics and 2Department of Molecular Biosciences, The University of Kansas, Lawrence, KS 66047, USA"},{"name":"1 Center for Bioinformatics and 2Department of Molecular Biosciences, The University of Kansas, Lawrence, KS 66047, USA"}]}],"member":"286","published-online":{"date-parts":[[2009,2,23]]},"reference":[{"key":"2023013110282461300_B1","doi-asserted-by":"crossref","first-page":"460","DOI":"10.1006\/jmbi.1995.0511","article-title":"Impact of local and non-local interactions on thermodynamics and kinetics of protein folding","volume":"252","author":"Abkevich","year":"1995","journal-title":"J. Mol. Biol."},{"key":"2023013110282461300_B2","doi-asserted-by":"crossref","first-page":"215","DOI":"10.1016\/j.str.2007.01.005","article-title":"Prediction of protein-protein association rates from a transition-state theory","volume":"15","author":"Alsallaq","year":"2007","journal-title":"Structure"},{"key":"2023013110282461300_B3","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1016\/S1359-0278(97)00024-2","article-title":"Direct evaluation of thermal fluctuations in proteins using a single-parameter harmonic potential","volume":"2","author":"Bahar","year":"1997","journal-title":"Fold. Des."},{"key":"2023013110282461300_B4","doi-asserted-by":"crossref","first-page":"8745","DOI":"10.1063\/1.459263","article-title":"How the range of pair interactions governs features of multidimensional potentials","volume":"93","author":"Braier","year":"1990","journal-title":"J. Chem. Phys."},{"key":"2023013110282461300_B5","doi-asserted-by":"crossref","first-page":"5897","DOI":"10.1063\/1.449621","article-title":"Structural and energetic effects of truncating long ranged interactions in ionic and polar fluids","volume":"83","author":"Brooks","year":"1985","journal-title":"J. Chem. Phys."},{"key":"2023013110282461300_B6","doi-asserted-by":"crossref","first-page":"167","DOI":"10.1002\/prot.340210302","article-title":"Funnels, pathways, and the energy landscape of protein folding: a synthesis","volume":"21","author":"Bryngelson","year":"1995","journal-title":"Proteins"},{"key":"2023013110282461300_B7","doi-asserted-by":"crossref","first-page":"6902","DOI":"10.1021\/j100356a007","article-title":"Intermediates and barrier crossing in a random energy model (with applications to protein folding)","volume":"93","author":"Bryngelson","year":"1989","journal-title":"J. Phys. Chem."},{"key":"2023013110282461300_B8","doi-asserted-by":"crossref","first-page":"862","DOI":"10.1110\/ps.03488704","article-title":"Orientational potentials extracted from protein structures improve native fold recognition","volume":"13","author":"Buchete","year":"2004","journal-title":"Prot. Sci."},{"key":"2023013110282461300_B9","doi-asserted-by":"crossref","first-page":"10636","DOI":"10.1073\/pnas.181147798","article-title":"Protein docking along smooth association pathways","volume":"98","author":"Camacho","year":"2001","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"2023013110282461300_B10","doi-asserted-by":"crossref","first-page":"1166","DOI":"10.1016\/S0006-3495(99)77281-4","article-title":"Free energy landscapes of encounter complexes in protein-protein association","volume":"76","author":"Camacho","year":"1999","journal-title":"Biophys. J."},{"key":"2023013110282461300_B11","doi-asserted-by":"crossref","first-page":"1166","DOI":"10.1110\/ps.8.6.1166","article-title":"Polymer principles and protein folding","volume":"8","author":"Dill","year":"1999","journal-title":"Prot. Sci."},{"key":"2023013110282461300_B12","doi-asserted-by":"crossref","first-page":"4859","DOI":"10.1088\/0953-4075\/29\/21\/002","article-title":"The effect of the range of the potential on the structure and stability of simple liquids: from clusters to bulk, from sodium to C60","volume":"29","author":"Doye","year":"1996","journal-title":"J. Phys. B At. Mol. Opt. Phys."},{"key":"2023013110282461300_B13","doi-asserted-by":"crossref","first-page":"282","DOI":"10.1002\/(SICI)1097-0134(199711)29:3<282::AID-PROT3>3.0.CO;2-D","article-title":"Local interactions and the optimization of protein folding","volume":"29","author":"Doyle","year":"1997","journal-title":"Proteins"},{"key":"2023013110282461300_B14","doi-asserted-by":"crossref","first-page":"1504","DOI":"10.1021\/jp003602d","article-title":"Computer simulation of protein-protein interactions","volume":"105","author":"Elcock","year":"2001","journal-title":"J. Phys. Chem. B"},{"key":"2023013110282461300_B15","doi-asserted-by":"crossref","first-page":"712","DOI":"10.1002\/prot.20521","article-title":"The Go model revisited: native structure and the geometric coupling between local and long-range contacts","volume":"60","author":"Faisca","year":"2005","journal-title":"Proteins"},{"key":"2023013110282461300_B16","doi-asserted-by":"crossref","first-page":"19819","DOI":"10.1073\/pnas.0709915104","article-title":"Localizing frustration in native proteins and protein assemblies","volume":"104","author":"Ferreiro","year":"2007","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"2023013110282461300_B17","doi-asserted-by":"crossref","first-page":"2370","DOI":"10.1073\/pnas.041614298","article-title":"The role of structure, energy landscape, dynamics, and allostery in the enzymatic function of myoglobin","volume":"98","author":"Frauenfelder","year":"2001","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"2023013110282461300_B18","doi-asserted-by":"crossref","first-page":"845","DOI":"10.1002\/prot.21714","article-title":"Dockground system of databases for protein recognition studies: unbound structures for docking","volume":"69","author":"Gao","year":"2007","journal-title":"Proteins"},{"key":"2023013110282461300_B19","doi-asserted-by":"crossref","first-page":"216","DOI":"10.1016\/0959-440X(95)80079-4","article-title":"Theory of electrostatic interactions in macromolecules","volume":"5","author":"Gilson","year":"1995","journal-title":"Curr. Opin. Struct. Biol."},{"key":"2023013110282461300_B20","doi-asserted-by":"crossref","first-page":"559","DOI":"10.1073\/pnas.75.2.559","article-title":"Respective roles of short- and long-range interactions in protein folding","volume":"75","author":"G\u014d","year":"1978","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"2023013110282461300_B21","doi-asserted-by":"crossref","first-page":"413","DOI":"10.1002\/prot.340220411","article-title":"Optimal local propensities for model proteins","volume":"22","author":"Govindarajan","year":"1995","journal-title":"Proteins"},{"key":"2023013110282461300_B22","doi-asserted-by":"crossref","first-page":"1843","DOI":"10.1110\/ps.8.9.1843","article-title":"Increasing protein stability by altering long-range Coulombic interactions","volume":"8","author":"Grimsley","year":"1999","journal-title":"Prot. Sci."},{"key":"2023013110282461300_B23","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1016\/S0301-4622(99)00010-1","article-title":"Importance of long-range interactions in protein folding","volume":"77","author":"Gromiha","year":"1999","journal-title":"Biophys. Chem."},{"key":"2023013110282461300_B24","doi-asserted-by":"crossref","first-page":"9617","DOI":"10.1063\/1.476437","article-title":"Correcting for electrostatic cutoffs in free energy simulations: toward consistency between simulations with different cutoffs","volume":"108","author":"Haluk","year":"1998","journal-title":"J. Chem. Phys."},{"key":"2023013110282461300_B25","doi-asserted-by":"crossref","first-page":"78","DOI":"10.1002\/prot.340050109","article-title":"Treatment of electrostatic effects in macromolecular modeling","volume":"5","author":"Harvey","year":"1989","journal-title":"Proteins"},{"key":"2023013110282461300_B26","doi-asserted-by":"crossref","first-page":"521","DOI":"10.1093\/bioinformatics\/btm625","article-title":"Structural flexibility in proteins: impact of the crystal environment","volume":"24","author":"Hinsen","year":"2008","journal-title":"Bioinformatics"},{"key":"2023013110282461300_B27","doi-asserted-by":"crossref","first-page":"344","DOI":"10.1002\/prot.21930","article-title":"The size of the intermolecular energy funnel in protein-protein interactions","volume":"72","author":"Hunjan","year":"2008","journal-title":"Proteins"},{"key":"2023013110282461300_B28","doi-asserted-by":"crossref","first-page":"10249","DOI":"10.1073\/pnas.1833310100","article-title":"Can energy landscape roughness of proteins and RNA be measured by using mechanical unfolding experiments?","volume":"100","author":"Hyeon","year":"2003","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"2023013110282461300_B29","doi-asserted-by":"crossref","first-page":"4711","DOI":"10.1021\/jp710339n","article-title":"Coarse-graining in interaction space: a systematic approach for replacing long-range electrostatics with short-range potentials","volume":"112","author":"Izvekov","year":"2008","journal-title":"J. Phys. Chem."},{"key":"2023013110282461300_B30","doi-asserted-by":"crossref","DOI":"10.1002\/047086334X","volume-title":"Intermolecular Interactions: Physical Picture, Computational Methods and Model Potentials.","author":"Kaplan","year":"2006"},{"key":"2023013110282461300_B31","doi-asserted-by":"crossref","first-page":"1223","DOI":"10.1016\/j.jmb.2004.01.002","article-title":"Can contact potentials reliably predict stability of proteins?","volume":"336","author":"Khatun","year":"2004","journal-title":"J. Mol. Biol."},{"key":"2023013110282461300_B32","doi-asserted-by":"crossref","first-page":"1719","DOI":"10.1126\/science.1067680","article-title":"Long-range interactions within a nonnative protein","volume":"295","author":"Klein-Seetharaman","year":"2002","journal-title":"Science"},{"key":"2023013110282461300_B33","doi-asserted-by":"crossref","first-page":"1113","DOI":"10.1099\/0022-1317-83-5-1113","article-title":"Long-range RNA-RNA interactions between distant regions of the hepatitis C virus internal ribosome entry site element","volume":"83","author":"Lafuente","year":"2002","journal-title":"J. Gen. Virol."},{"key":"2023013110282461300_B34","doi-asserted-by":"crossref","first-page":"32","DOI":"10.1002\/prot.340060104","article-title":"The effects of truncating long-range forces on protein dynamics","volume":"6","author":"Loncharich","year":"1989","journal-title":"Proteins"},{"key":"2023013110282461300_B35","doi-asserted-by":"crossref","first-page":"178101","DOI":"10.1103\/PhysRevLett.97.178101","article-title":"Statistically enhanced self-attraction of random patterns","volume":"97","author":"Lukatsky","year":"2006","journal-title":"Phys. Rev. Lett."},{"key":"2023013110282461300_B36","doi-asserted-by":"crossref","first-page":"2166","DOI":"10.1002\/pro.5560061011","article-title":"Ligand binding to proteins: the binding landscape model","volume":"6","author":"Miller","year":"1997","journal-title":"Prot. Sci."},{"key":"2023013110282461300_B37","doi-asserted-by":"crossref","first-page":"328","DOI":"10.1063\/1.478067","article-title":"Structural relaxation in Morse clusters: energy landscapes","volume":"110","author":"Miller","year":"1999","journal-title":"J. Chem. Phys."},{"key":"2023013110282461300_B38","doi-asserted-by":"crossref","first-page":"L25","DOI":"10.1529\/biophysj.105.069336","article-title":"The entropic cost of protein-protein association: A case study on acetylcholinesterase binding to fasciculin-2","volume":"89","author":"Minh","year":"2005","journal-title":"Biophys. J.: Biophys. Lett."},{"key":"2023013110282461300_B39","doi-asserted-by":"crossref","first-page":"482","DOI":"10.1038\/sj.embor.7400403","article-title":"Direct measurement of protein energy landscape roughness","volume":"6","author":"Nevo","year":"2005","journal-title":"EMBO Rep."},{"key":"2023013110282461300_B40","doi-asserted-by":"crossref","first-page":"1537","DOI":"10.1016\/S0006-3495(00)76405-8","article-title":"On the truncation of long-range electrostatic interactions in DNA","volume":"79","author":"Norberg","year":"2000","journal-title":"Biophys. J."},{"key":"2023013110282461300_B41","doi-asserted-by":"crossref","first-page":"144","DOI":"10.1002\/prot.21665","article-title":"Large-scale characteristics of the energy landscape in protein-protein interactions","volume":"71","author":"O'Toole","year":"2008","journal-title":"Proteins"},{"key":"2023013110282461300_B42","doi-asserted-by":"crossref","first-page":"50","DOI":"10.1038\/5891","article-title":"A potential smoothing algorithm accurately predicts transmembrane helix packing","volume":"6","author":"Pappu","year":"1999","journal-title":"Nat. Struct. Biol."},{"key":"2023013110282461300_B43","doi-asserted-by":"crossref","first-page":"361","DOI":"10.1007\/s10822-007-9116-0","article-title":"Calculations of protein-ligand binding entropy of relative and overall molecular motions","volume":"21","author":"Ruvinsky","year":"2007","journal-title":"J. Comput. Aided Mol. Des."},{"key":"2023013110282461300_B44","doi-asserted-by":"crossref","first-page":"845","DOI":"10.1002\/prot.20385","article-title":"The key role of atom types, reference states, and interaction cutoff radii in the knowledge-based method: new variational approach","volume":"58","author":"Ruvinsky","year":"2005","journal-title":"Proteins"},{"key":"2023013110282461300_B45","doi-asserted-by":"crossref","first-page":"1089","DOI":"10.1002\/jcc.20246","article-title":"New and fast statistical-thermodynamic method for computation of protein-ligand binding entropy substantially improves docking accuracy","volume":"26","author":"Ruvinsky","year":"2005","journal-title":"J. Comput. Chem."},{"key":"2023013110282461300_B46","doi-asserted-by":"crossref","first-page":"1498","DOI":"10.1002\/prot.21644","article-title":"Interaction cutoff effect on ruggedness of protein-protein energy landscape","volume":"70","author":"Ruvinsky","year":"2008","journal-title":"Proteins"},{"key":"2023013110282461300_B47","doi-asserted-by":"crossref","first-page":"2150","DOI":"10.1529\/biophysj.108.132977","article-title":"Chasing funnels on protein-protein energy landscapes at different resolutions","volume":"95","author":"Ruvinsky","year":"2008","journal-title":"Biophys. J."},{"key":"2023013110282461300_B48","doi-asserted-by":"crossref","first-page":"155","DOI":"10.1146\/annurev.biophys.28.1.155","article-title":"Molecular dynamics simulations of biomolecules: long-range electrostatic effects","volume":"28","author":"Sagui","year":"1999","journal-title":"Ann. Rev. Biophys. Biomol. Struct."},{"key":"2023013110282461300_B49","doi-asserted-by":"crossref","first-page":"6106","DOI":"10.1063\/1.459003","article-title":"Cluster optimization simplified by interaction modification","volume":"93","author":"Stillinger","year":"1990","journal-title":"J. Chem. Phys."},{"key":"2023013110282461300_B50","doi-asserted-by":"crossref","first-page":"19825","DOI":"10.1073\/pnas.0709922104","article-title":"Consequences of localized frustration for the folding mechanism of the IM7 protein","volume":"104","author":"Sutto","year":"2007","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"2023013110282461300_B51","doi-asserted-by":"crossref","first-page":"1905","DOI":"10.1103\/PhysRevLett.77.1905","article-title":"Large amplitude elastic motions in proteins from a single-parameter, atomic analysis","volume":"77","author":"Tirion","year":"1996","journal-title":"Phys. Rev. Lett."},{"key":"2023013110282461300_B52","doi-asserted-by":"crossref","first-page":"40","DOI":"10.1002\/1097-0134(20001001)41:1<40::AID-PROT70>3.0.CO;2-U","article-title":"Distance-dependent, pair potential for protein folding: Results from linear optimization","volume":"41","author":"Tobi","year":"2000","journal-title":"Proteins"},{"key":"2023013110282461300_B53","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1002\/(SICI)1097-0134(20000701)40:1<71::AID-PROT90>3.0.CO;2-3","article-title":"On the design and analysis of protein folding potentials","volume":"40","author":"Tobi","year":"2000","journal-title":"Proteins"},{"key":"2023013110282461300_B54","doi-asserted-by":"crossref","first-page":"1572","DOI":"10.1110\/ps.8701","article-title":"How common is the funnel-like energy landscape in protein-protein interactions?","volume":"10","author":"Tovchigrechko","year":"2001","journal-title":"Prot. Sci."},{"key":"2023013110282461300_B55","doi-asserted-by":"crossref","first-page":"296","DOI":"10.1002\/prot.20573","article-title":"Development and testing of an automated approach to protein docking","volume":"60","author":"Tovchigrechko","year":"2005","journal-title":"Proteins"},{"key":"2023013110282461300_B56","doi-asserted-by":"crossref","first-page":"1888","DOI":"10.1110\/ps.4730102","article-title":"Docking of protein models","volume":"11","author":"Tovchigrechko","year":"2002","journal-title":"Prot. Sci."},{"key":"2023013110282461300_B57","doi-asserted-by":"crossref","first-page":"1181","DOI":"10.1110\/ps.8.6.1181","article-title":"Folding funnels, binding funnels, and protein function","volume":"8","author":"Tsai","year":"1999","journal-title":"Prot. Sci."},{"key":"2023013110282461300_B58","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1093\/protein\/9.1.37","article-title":"Long-distance potentials: an approach to the multiple-minima problem in ligand-receptor interaction","volume":"9","author":"Vakser","year":"1996","journal-title":"Prot. Eng."},{"key":"2023013110282461300_B59","doi-asserted-by":"crossref","first-page":"313","DOI":"10.1016\/S0076-6879(02)43144-8","article-title":"Strategies for modeling the interactions of the transmembrane helices of G-protein coupled receptors by geometric complementarity using the GRAMM computer algorithm","volume":"343","author":"Vakser","year":"2002","journal-title":"Methods Enzymol."},{"key":"2023013110282461300_B60","doi-asserted-by":"crossref","first-page":"8477","DOI":"10.1073\/pnas.96.15.8477","article-title":"A systematic study of low-resolution recognition in protein-protein complexes","volume":"96","author":"Vakser","year":"1999","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"2023013110282461300_B61","doi-asserted-by":"crossref","first-page":"11101","DOI":"10.1063\/1.477748","article-title":"Pairwise contact potentials are unsuitable for protein folding","volume":"109","author":"Vendruscolo","year":"1998","journal-title":"J. Chem. Phys."},{"key":"2023013110282461300_B62","doi-asserted-by":"crossref","first-page":"656","DOI":"10.1103\/PhysRevLett.82.656","article-title":"Protein folding in contact map space","volume":"82","author":"Vendruscolo","year":"1999","journal-title":"Phys. Rev. Lett."},{"key":"2023013110282461300_B63","doi-asserted-by":"crossref","first-page":"188101","DOI":"10.1103\/PhysRevLett.90.188101","article-title":"Energy landscape theory, funnels, specificity, and optimal criterion of biomolecular binding","volume":"90","author":"Wang","year":"2003","journal-title":"Phys. Rev. Lett."},{"key":"2023013110282461300_B64","doi-asserted-by":"crossref","first-page":"L109","DOI":"10.1529\/biophysj.107.105551","article-title":"Optimal specificity and function for flexible biomolecular recognition","volume":"92","author":"Wang","year":"2007","journal-title":"Biophys. J."},{"key":"2023013110282461300_B65","doi-asserted-by":"crossref","first-page":"5138","DOI":"10.1021\/j100191a071","article-title":"Application of the diffusion equation method of global optimization to water clusters","volume":"96","author":"Wawak","year":"1992","journal-title":"J. Phys. Chem."},{"key":"2023013110282461300_B66","doi-asserted-by":"crossref","first-page":"1100","DOI":"10.1002\/jcc.10106","article-title":"Gravitational smoothing as a global optimization strategy","volume":"23","author":"Whitfield","year":"2002","journal-title":"J. Comput. Chem."},{"key":"2023013110282461300_B67","doi-asserted-by":"crossref","first-page":"405","DOI":"10.1017\/S0033583505004075","article-title":"Recent successes of the energy landscape theory of protein folding and function","volume":"38","author":"Wolynes","year":"2005","journal-title":"Quart. Rev. Biophys."}],"container-title":["Bioinformatics"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/academic.oup.com\/bioinformatics\/article-pdf\/25\/9\/1132\/48985276\/bioinformatics_25_9_1132.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/academic.oup.com\/bioinformatics\/article-pdf\/25\/9\/1132\/48985276\/bioinformatics_25_9_1132.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,1,31]],"date-time":"2023-01-31T20:35:36Z","timestamp":1675197336000},"score":1,"resource":{"primary":{"URL":"https:\/\/academic.oup.com\/bioinformatics\/article\/25\/9\/1132\/203514"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2009,2,23]]},"references-count":67,"journal-issue":{"issue":"9","published-print":{"date-parts":[[2009,5,1]]}},"URL":"https:\/\/doi.org\/10.1093\/bioinformatics\/btp108","relation":{},"ISSN":["1367-4811","1367-4803"],"issn-type":[{"value":"1367-4811","type":"electronic"},{"value":"1367-4803","type":"print"}],"subject":[],"published-other":{"date-parts":[[2009,5,1]]},"published":{"date-parts":[[2009,2,23]]}}}