{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,21]],"date-time":"2026-09-21T10:08:46Z","timestamp":1789985326685,"version":"4.0.1"},"reference-count":65,"publisher":"Oxford University Press (OUP)","issue":"4","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2005,10,1]]},"DOI":"10.1093\/jb\/mvi131","type":"journal-article","created":{"date-parts":[[2005,11,4]],"date-time":"2005-11-04T08:07:38Z","timestamp":1131091658000},"page":"335-341","source":"Crossref","is-referenced-by-count":28,"title":["Influence of Fluoro, Chloro and Alkyl Alcohols on the Folding Pathway of Human Serum Albumin"],"prefix":"10.1093","volume":"138","author":[{"given":"Yogesh","family":"Kumar","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Salman","family":"Muzammil","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Saad","family":"Tayyab","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2005,10]]},"reference":[{"key":"key\n\t\t\t\t20171010193953_B1","doi-asserted-by":"crossref","unstructured":"Kuwajima, K. (1989) The molten globule state as a clue for understanding the folding and cooperativity of globular proteins. Proteins: Struct. Funct. Genet.6, 87\u2013103","DOI":"10.1002\/prot.340060202"},{"key":"key\n\t\t\t\t20171010193953_B2","doi-asserted-by":"crossref","unstructured":"Goto, Y., Takahashi, N., and Fink, A.L. (1990) Mechanism of acid-induced folding of proteins. Biochemistry29, 3480\u20133488","DOI":"10.1021\/bi00466a009"},{"key":"key\n\t\t\t\t20171010193953_B3","doi-asserted-by":"crossref","unstructured":"Dill, K.A. and Shortle, D. (1991) Denatured states of proteins. Annu. Rev. Biochem.60, 795\u2013825","DOI":"10.1146\/annurev.bi.60.070191.004051"},{"key":"key\n\t\t\t\t20171010193953_B4","doi-asserted-by":"crossref","unstructured":"Fink, A.L., Calciano, L.J., Goto, Y., Kurotsu, T., and Palleros, D.R. (1994) Classification of acid denaturation of proteins: intermediates and unfolded states. Biochemistry33, 12504\u201312511","DOI":"10.1021\/bi00207a018"},{"key":"key\n\t\t\t\t20171010193953_B5","doi-asserted-by":"crossref","unstructured":"Konno, T., Iwashita, J., and Nagayama, K. (2000) Fluorinated alcohol, the third group of cosolvents that stabilize the molten-globule state relative to a highly denatured state of cytochrome c. Protein Sci.9, 564\u2013569","DOI":"10.1110\/ps.9.3.564"},{"key":"key\n\t\t\t\t20171010193953_B6","doi-asserted-by":"crossref","unstructured":"Roder, H. and Colon, W. (1997) Kinetic role of early intermediates in protein folding. Curr. Opin. Struct. Biol.7, 15\u201328","DOI":"10.1016\/S0959-440X(97)80004-8"},{"key":"key\n\t\t\t\t20171010193953_B7","doi-asserted-by":"crossref","unstructured":"Kim, P.S. and Baldwin, R.L. (1990) Intermediates in the folding reactions of small proteins. Annu. Rev. Biochem.59, 631\u2013660","DOI":"10.1146\/annurev.bi.59.070190.003215"},{"key":"key\n\t\t\t\t20171010193953_B8","unstructured":"Schmid, F.X. (1992) Kinetics of unfolding and refolding of single-domain proteins. in Protein Folding (Creighton, T.E., ed.) pp. 197\u2013241, W.H. Freeman, New York"},{"key":"key\n\t\t\t\t20171010193953_B9","doi-asserted-by":"crossref","unstructured":"Matthews, C.R. (1993) Pathways of protein folding. Annu. Rev. Biochem.62, 653\u2013683","DOI":"10.1146\/annurev.bi.62.070193.003253"},{"key":"key\n\t\t\t\t20171010193953_B10","doi-asserted-by":"crossref","unstructured":"Evans, P.A. and Radford, S.E. (1994) Probing the structure of folding intermediates. Curr. Opin. Struct. Biol.4, 100\u2013106","DOI":"10.1016\/S0959-440X(94)90066-3"},{"key":"key\n\t\t\t\t20171010193953_B11","doi-asserted-by":"crossref","unstructured":"Plaxco, K.W. and Dobson, C.M. (1996) Time-resolved biophysical methods in the study of protein folding. Curr. Opin. Struct. Biol.6, 630\u2013636","DOI":"10.1016\/S0959-440X(96)80029-7"},{"key":"key\n\t\t\t\t20171010193953_B12","unstructured":"Uversky, V.N. and Ptitsyn, O.B. (1994) \u201cPartly folded\u201d state, a new equilibrium state of protein molecules: four-state guanidinium chloride-induced unfolding of beta-lactamase at low temperature. Biochemistry33, 2782\u20132791"},{"key":"key\n\t\t\t\t20171010193953_B13","doi-asserted-by":"crossref","unstructured":"Dobson, C.M. (1992) Resting places on folding pathways. Curr. Biol.2, 343\u2013345","DOI":"10.1016\/0960-9822(92)90047-E"},{"key":"key\n\t\t\t\t20171010193953_B14","doi-asserted-by":"crossref","unstructured":"Ptitsyn, O.B. (1995) Molten globule and protein folding. Adv. Protein Chem.47, 83\u2013229","DOI":"10.1016\/S0065-3233(08)60546-X"},{"key":"key\n\t\t\t\t20171010193953_B15","doi-asserted-by":"crossref","unstructured":"Goldberg, M.E. (1969) Tertiary structure of Escherichia coli \u03b2-D-galactosidase. J. Mol. Biol.46, 441\u2013446","DOI":"10.1016\/0022-2836(69)90187-9"},{"key":"key\n\t\t\t\t20171010193953_B16","doi-asserted-by":"crossref","unstructured":"Wetlaufer, D.B. (1973) Nucleation, rapid folding and globular intrachain regions in proteins. Proc. Natl Acad. Sci. USA70, 697\u2013701","DOI":"10.1073\/pnas.70.3.697"},{"key":"key\n\t\t\t\t20171010193953_B17","doi-asserted-by":"crossref","unstructured":"Wetlaufer, D.B. (1981) Folding of protein fragments. Adv. Protein Chem.34, 61\u201392","DOI":"10.1016\/S0065-3233(08)60518-5"},{"key":"key\n\t\t\t\t20171010193953_B18","doi-asserted-by":"crossref","unstructured":"Janin, J. and Wodak, S.J. (1983) Structural domains in protein and their role in the dynamics of protein function. Prog. Biophys. Mol. Biol.42, 21\u201378","DOI":"10.1016\/0079-6107(83)90003-2"},{"key":"key\n\t\t\t\t20171010193953_B19","doi-asserted-by":"crossref","unstructured":"Jaenicke, R. (1996) Protein folding and association: in vitro studies for self-organization and targeting in the cell. Curr. Top. Cell Reg.34, 209\u2013314","DOI":"10.1016\/S0070-2137(96)80008-2"},{"key":"key\n\t\t\t\t20171010193953_B20","doi-asserted-by":"crossref","unstructured":"Kuwajima, K. (1996) The molten globule state of alpha-lactalbumin. FASEB J.10, 102\u2013109","DOI":"10.1096\/fasebj.10.1.8566530"},{"key":"key\n\t\t\t\t20171010193953_B21","doi-asserted-by":"crossref","unstructured":"Hughson, F.M., Wright, P.E., and Baldwin, R.L. (1990) Structural characterization of a partly folded apomyoglobin intermediate. Science249, 1544\u20131548","DOI":"10.1126\/science.2218495"},{"key":"key\n\t\t\t\t20171010193953_B22","doi-asserted-by":"crossref","unstructured":"Buck, M., Radford, S.E., and Dobson, C.M. (1993) A partially folded state of HEWL in TFE: structural characterization and implications for protein folding. Biochemistry32, 669\u2013678","DOI":"10.1021\/bi00053a036"},{"key":"key\n\t\t\t\t20171010193953_B23","unstructured":"Herskovits, T.T., Gadegbeku, B., and Jaillet, H. (1970) On the structural stability and solvent denaturation of proteins. I. Denaturation by the alcohols and glycols. J. Biol. Chem.245, 2588\u20132598"},{"key":"key\n\t\t\t\t20171010193953_B24","doi-asserted-by":"crossref","unstructured":"Galat, A. (1985) Early stages in the trifluoroethanol-induced unfolding of hen egg-white lysozyme and its complex with (GlcNAc)3. Biochim. Biophys. Acta827, 221\u2013227","DOI":"10.1016\/0167-4838(85)90206-7"},{"key":"key\n\t\t\t\t20171010193953_B25","doi-asserted-by":"crossref","unstructured":"Nelson, J.W. and Kallenbach, N.R. (1986) Stabilization of the ribonuclease S-peptide \u03b1-helix by trifluoroethanol solutions. Proteins: Struct. Funct. Genet.1, 211\u2013217","DOI":"10.1002\/prot.340010303"},{"key":"key\n\t\t\t\t20171010193953_B26","doi-asserted-by":"crossref","unstructured":"Shiraki, K., Nishikawa, K., and Goto, Y. (1995) Trifluoroethanol-induced stabilization of the alpha-helical structure of beta-lactoglobulin: implication for non-hierarchical protein folding. J. Mol. Biol.245, 180\u2013194","DOI":"10.1006\/jmbi.1994.0015"},{"key":"key\n\t\t\t\t20171010193953_B27","doi-asserted-by":"crossref","unstructured":"Alexandrescu, A.T., Ng, Y.L., and Dobson, C.M. (1994) Characterization of a trifluoroethanol-induced partially folded state of alpha-lactalbumin. J. Mol. Biol.235, 587\u2013599","DOI":"10.1006\/jmbi.1994.1015"},{"key":"key\n\t\t\t\t20171010193953_B28","doi-asserted-by":"crossref","unstructured":"Nishii, I., Kataoka, M., Tokunaga, F., and Goto, Y. (1994) Cold denaturation of the molten globule states of apomyoglobin and a profile for protein folding. Biochemistry33, 4903\u20134909","DOI":"10.1021\/bi00182a019"},{"key":"key\n\t\t\t\t20171010193953_B29","doi-asserted-by":"crossref","unstructured":"Hagihara, Y., Tan, Y., and Goto, Y. (1994) Comparison of the conformational stability of the molten globule and native states of horse cytochrome c. Effects of acetylation, heat, urea and guanidine-hydrochloride. J. Mol. Biol.237, 336\u2013348","DOI":"10.1006\/jmbi.1994.1234"},{"key":"key\n\t\t\t\t20171010193953_B30","doi-asserted-by":"crossref","unstructured":"Peters, T., Jr. (1985) Serum albumin. Adv. Protein Chem.37, 161\u2013245","DOI":"10.1016\/S0065-3233(08)60065-0"},{"key":"key\n\t\t\t\t20171010193953_B31","doi-asserted-by":"crossref","unstructured":"Pace, C.N., Vajdos, F., Fee, L., Grimsley, G., and Gray, T. (1995) How to measure and predict the molar absorption coefficient of a protein. Protein Sci.4, 2411\u20132423","DOI":"10.1002\/pro.5560041120"},{"key":"key\n\t\t\t\t20171010193953_B32","doi-asserted-by":"crossref","unstructured":"Mulqueen, P.M. and Kronman, M.J. (1982) Binding of naphthalene dyes to the N and A conformers of bovine alpha-lactalbumin. Arch. Biochem. Biophys.215, 28\u201339","DOI":"10.1016\/0003-9861(82)90275-2"},{"key":"key\n\t\t\t\t20171010193953_B33","doi-asserted-by":"crossref","unstructured":"Warren, J.R. and Gordon, J.A. (1966) On the refractive indices of aqueous solutions of urea. J. Phys. Chem.70, 297\u2013300","DOI":"10.1021\/j100873a507"},{"key":"key\n\t\t\t\t20171010193953_B34","doi-asserted-by":"crossref","unstructured":"Nozaki, Y. (1972) The preparation of guanidine hydrochloride. Methods Enzymol.26, 43\u201350","DOI":"10.1016\/S0076-6879(72)26005-0"},{"key":"key\n\t\t\t\t20171010193953_B35","doi-asserted-by":"crossref","unstructured":"Pace, C.N. and Scholtz, J.M. (1997) Measuring the conformational stability of a protein. In Protein Structure: A Practical Approach (Creighton, T.E., ed.) pp. 299\u2013321, Oxford University Press, New York","DOI":"10.1093\/oso\/9780199636198.003.0012"},{"key":"key\n\t\t\t\t20171010193953_B36","doi-asserted-by":"crossref","unstructured":"Tanford, C. (1968) Protein denaturation. Adv. Protein Chem.23, 121\u2013282","DOI":"10.1016\/S0065-3233(08)60401-5"},{"key":"key\n\t\t\t\t20171010193953_B37","doi-asserted-by":"crossref","unstructured":"Pace, C.N. (1986) Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol.131, 266\u2013280","DOI":"10.1016\/0076-6879(86)31045-0"},{"key":"key\n\t\t\t\t20171010193953_B38","doi-asserted-by":"crossref","unstructured":"Muzammil, S., Kumar, Y., and Tayyab, S. (2000) Anion-induced stabilization of human serum albumin prevents the formation of intermediate during urea denaturation. Proteins: Struct. Funct. Genet.40, 29\u201338","DOI":"10.1002\/(SICI)1097-0134(20000701)40:1<29::AID-PROT50>3.0.CO;2-P"},{"key":"key\n\t\t\t\t20171010193953_B39","doi-asserted-by":"crossref","unstructured":"Khan, M.Y., Agrawal, S.K., and Hangloo, S. (1987) Urea-induced structural transformations in bovine serum albumin. J. Biochem.102, 313\u2013317","DOI":"10.1093\/oxfordjournals.jbchem.a122056"},{"key":"key\n\t\t\t\t20171010193953_B40","doi-asserted-by":"crossref","unstructured":"Ahmad, N. and Qasim, M.A. (1995) Fatty acid binding to bovine serum albumin prevents formation of intermediate during denaturation. Eur. J. Biochem.227, 563\u2013565","DOI":"10.1111\/j.1432-1033.1995.tb20425.x"},{"key":"key\n\t\t\t\t20171010193953_B41","doi-asserted-by":"crossref","unstructured":"Tayyab, S., Sharma, N., and Khan, M.M. (2000) Use of domain specific ligands to study urea-induced unfolding of bovine serum albumin. Biochem. Biophys. Res. Commun.277, 83\u201388","DOI":"10.1006\/bbrc.2000.3642"},{"key":"key\n\t\t\t\t20171010193953_B42","doi-asserted-by":"crossref","unstructured":"Jirgensons, B. (1967) Effects of n-propyl alcohol and detergents on the optical rotatory dispersion of \u03b1-chymotrypsinogen, \u03b2-casein, histone fraction F1, and soybean trypsin inhibitor. J. Biol. Chem.242, 912\u2013918","DOI":"10.1016\/S0021-9258(18)96212-5"},{"key":"key\n\t\t\t\t20171010193953_B43","doi-asserted-by":"crossref","unstructured":"Ohama, H., Sugiura, N., Tanaka, F., and Yagi, K. (1977) Effect of alcohols on the structure and function of D-amino-acid oxidase. Biochemistry16, 126\u2013131","DOI":"10.1021\/bi00620a021"},{"key":"key\n\t\t\t\t20171010193953_B44","doi-asserted-by":"crossref","unstructured":"Asakura, T., Adachi, K., and Schwartz, E. (1978) Stabilizing effect of various organic solvents on protein. J. Biol. Chem.253, 6423\u20136425","DOI":"10.1016\/S0021-9258(19)46949-4"},{"key":"key\n\t\t\t\t20171010193953_B45","doi-asserted-by":"crossref","unstructured":"Stockman, B.J., Euvrard, A., and Scahill, T.A. (1993) Heteronuclear three-dimensional NMR spectroscopy of a partially denatured protein: the A-state of human ubiquitin. J. Biomol. NMR3, 285\u2013296","DOI":"10.1007\/BF00212515"},{"key":"key\n\t\t\t\t20171010193953_B46","doi-asserted-by":"crossref","unstructured":"Alexandrescu, A.T., Evans, P.A., Pitkeathly, M., Baum, J., and Dobson, C.M. (1993) Structure and dynamics of the acid-denatured molten globule state of alpha-lactalbumin: a two-dimensional NMR study. Biochemistry32, 1707\u20131718","DOI":"10.1021\/bi00058a003"},{"key":"key\n\t\t\t\t20171010193953_B47","doi-asserted-by":"crossref","unstructured":"Chiti, F., Taddei, N., Webster, P., Hamada, D., Flaschi, T., Ramponi, G., and Dobson, C.M. (1999) Acceleration of the folding of acylphosphatase by stabilization of local secondary structure. Nat. Struct. Biol.6, 380\u2013387","DOI":"10.1038\/7616"},{"key":"key\n\t\t\t\t20171010193953_B48","doi-asserted-by":"crossref","unstructured":"Hamada, D., Chiti, F., Guijarro, J.I., Kataoka, M., Taddei, N., and Dobson, C.M. (2000) Evidence concerning rate-limiting steps in protein folding from the effects of trifluoroethanol. Nat. Struct. Biol.7, 58\u201361","DOI":"10.1038\/71259"},{"key":"key\n\t\t\t\t20171010193953_B49","doi-asserted-by":"crossref","unstructured":"Hermans, J., Jr. (1966) The effect of protein denaturants on the stability of the \u03b1 helix. J. Am. Chem. Soc.88, 2418\u20132422","DOI":"10.1021\/ja00963a010"},{"key":"key\n\t\t\t\t20171010193953_B50","doi-asserted-by":"crossref","unstructured":"Kumar, Y., Tayyab, S. and Muzammil, S. (2004) Molten-globule like partially folded states of human serum albumin induced by fluoro and alkyl alcohols at low pH. Arch. Biochem. Biophys.426, 3\u201310","DOI":"10.1016\/j.abb.2004.03.025"},{"key":"key\n\t\t\t\t20171010193953_B51","doi-asserted-by":"crossref","unstructured":"Goldammer, E.V. and Hertz, H.G. (1970) Molecular motion and structure of aqueous mixtures with nonelectrolytes as studied by nuclear magnetic relaxation methods. J. Phys. Chem.74, 3734\u20133755","DOI":"10.1021\/j100715a008"},{"key":"key\n\t\t\t\t20171010193953_B52","doi-asserted-by":"crossref","unstructured":"Ben-Naim, A. (1980) in Hydrophobic Interaction, pp. 81\u221282, Plenum Press, New York","DOI":"10.1007\/978-1-4684-3545-0"},{"key":"key\n\t\t\t\t20171010193953_B53","doi-asserted-by":"crossref","unstructured":"Arakawa, T. and Goddette, D. (1985) The mechanism of helical transition of proteins by organic solvents. Arch. Biochem. Biophys.240, 21\u201332","DOI":"10.1016\/0003-9861(85)90004-9"},{"key":"key\n\t\t\t\t20171010193953_B54","doi-asserted-by":"crossref","unstructured":"von Hippel, P.H. and Wong, K.-Y. (1965) On the Conformational Stability of Globular Proteins. The effects of various electrolytes and nonelectrolytes on the thermal ribonuclease transition. J. Biol. Chem.240, 3909\u20133923","DOI":"10.1016\/S0021-9258(18)97128-0"},{"key":"key\n\t\t\t\t20171010193953_B55","doi-asserted-by":"crossref","unstructured":"Parodi, R.M., Bianchi, E., and Ciferri, A. (1973) Thermodynamics of unfolding of lysozyme in aqueous alcohol solutions. J. Biol. Chem.248, 4047\u20134051","DOI":"10.1016\/S0021-9258(19)43836-2"},{"key":"key\n\t\t\t\t20171010193953_B56","doi-asserted-by":"crossref","unstructured":"He, X.M. and Carter D.C. (1992) Atomic structure and chemistry of human serum albumin. Nature358, 209\u2013215","DOI":"10.1038\/358209a0"},{"key":"key\n\t\t\t\t20171010193953_B57","doi-asserted-by":"crossref","unstructured":"Sugio, S., Kashima, A., Mochizuki, S., Noda, M., and Kobayashi, K. (1999) Crystal structure of human serum albumin at 2.5 \u00c5 resolution. Protein Eng.12, 439\u2013446","DOI":"10.1093\/protein\/12.6.439"},{"key":"key\n\t\t\t\t20171010193953_B58","doi-asserted-by":"crossref","unstructured":"Eggers, D.K. and Valentine, J.S. (2001) Crowding and hydration effects on protein conformation: a study with sol-gel encapsulated proteins. J. Mol. Biol.314, 911\u2013922","DOI":"10.1006\/jmbi.2001.5166"},{"key":"key\n\t\t\t\t20171010193953_B59","doi-asserted-by":"crossref","unstructured":"Pace, C.N. (1990) Measuring and increasing protein stability. Trends. Biotech.8, 93\u201398","DOI":"10.1016\/0167-7799(90)90146-O"},{"key":"key\n\t\t\t\t20171010193953_B60","doi-asserted-by":"crossref","unstructured":"Greene, R.F. and Pace, C.N. (1974) Urea and guanidine hydrochloride denaturation of ribonuclease, lysozyme, \u03b1-chymotrypsin and \u03b2-lactoglobulin. J. Biol. Chem.249, 5388\u20135393","DOI":"10.1016\/S0021-9258(20)79739-5"},{"key":"key\n\t\t\t\t20171010193953_B61","doi-asserted-by":"crossref","unstructured":"Robinson, D.R. and Jencks, W.P. (1965) The effect of compounds of the urea-guanidinium class on the activity coefficients of acetyltetraglycine ethyl ester and related compounds. J. Am. Chem. Soc.87, 2462\u20132470","DOI":"10.1021\/ja01089a028"},{"key":"key\n\t\t\t\t20171010193953_B62","doi-asserted-by":"crossref","unstructured":"Schellman, J.A. (1987) Selective binding and solvent denaturation. Biopolymers26, 549\u2013559","DOI":"10.1002\/bip.360260408"},{"key":"key\n\t\t\t\t20171010193953_B63","doi-asserted-by":"crossref","unstructured":"Alonso, D.O. and Dill, K.A. (1991) Solvent denaturation and stabilization of globular proteins. Biochemistry30, 5974\u20135985","DOI":"10.1021\/bi00238a023"},{"key":"key\n\t\t\t\t20171010193953_B64","doi-asserted-by":"crossref","unstructured":"Mayo, S.L. and Baldwin, R.L. (1993) Guanidinium chloride induction of partial unfolding in amide proton exchange in RNAse A. Science262, 873\u2013876","DOI":"10.1126\/science.8235609"},{"key":"key\n\t\t\t\t20171010193953_B65","doi-asserted-by":"crossref","unstructured":"Monera, O.D., Kay, C.M., and Hodges, R.S. (1994) Protein denaturation with guanidine hydrochloride or urea provides a different estimate of stability depending on the contributions of electrostatic interactions. Protein Sci.3, 1984\u20131991","DOI":"10.1002\/pro.5560031110"}],"container-title":["The Journal of Biochemistry"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/academic.oup.com\/jb\/article-pdf\/138\/4\/335\/2468632\/mvi131.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2024,1,31]],"date-time":"2024-01-31T12:21:48Z","timestamp":1706703708000},"score":1,"resource":{"primary":{"URL":"http:\/\/academic.oup.com\/jb\/article\/138\/4\/335\/828060\/Influence-of-Fluoro-Chloro-and-Alkyl-Alcohols-on"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2005,10,1]]},"references-count":65,"journal-issue":{"issue":"4","published-online":{"date-parts":[[2005,10]]},"published-print":{"date-parts":[[2005,10,1]]}},"URL":"https:\/\/doi.org\/10.1093\/jb\/mvi131","relation":{},"ISSN":["1756-2651","0021-924X"],"issn-type":[{"value":"1756-2651","type":"electronic"},{"value":"0021-924X","type":"print"}],"subject":[],"published-other":{"date-parts":[[2005,10]]},"published":{"date-parts":[[2005,10,1]]}}}