{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,7]],"date-time":"2026-05-07T04:57:37Z","timestamp":1778129857586,"version":"3.51.4"},"reference-count":48,"publisher":"Springer Science and Business Media LLC","issue":"12","license":[{"start":{"date-parts":[[2010,10,17]],"date-time":"2010-10-17T00:00:00Z","timestamp":1287273600000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/www.springer.com\/tdm"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Nat Chem Biol"],"published-print":{"date-parts":[[2010,12]]},"DOI":"10.1038\/nchembio.455","type":"journal-article","created":{"date-parts":[[2010,10,17]],"date-time":"2010-10-17T14:10:01Z","timestamp":1287324601000},"page":"914-920","source":"Crossref","is-referenced-by-count":214,"title":["The kinetic parameters and energy cost of the Hsp70 chaperone as a polypeptide unfoldase"],"prefix":"10.1038","volume":"6","author":[{"given":"Sandeep K","family":"Sharma","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Paolo","family":"De Los Rios","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Philipp","family":"Christen","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ariel","family":"Lustig","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Pierre","family":"Goloubinoff","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"297","published-online":{"date-parts":[[2010,10,17]]},"reference":[{"key":"BFnchembio455_CR1","doi-asserted-by":"publisher","first-page":"223","DOI":"10.1126\/science.181.4096.223","volume":"181","author":"CB Anfinsen","year":"1973","unstructured":"Anfinsen, C.B. Principles that govern folding of protein chains. Science 181, 223\u2013230 (1973).","journal-title":"Science"},{"key":"BFnchembio455_CR2","doi-asserted-by":"publisher","first-page":"884","DOI":"10.1038\/nature02261","volume":"426","author":"CM Dobson","year":"2003","unstructured":"Dobson, C.M. Protein folding and misfolding. Nature 426, 884\u2013890 (2003).","journal-title":"Nature"},{"key":"BFnchembio455_CR3","doi-asserted-by":"publisher","first-page":"475","DOI":"10.1038\/372475a0","volume":"372","author":"DA Parsell","year":"1994","unstructured":"Parsell, D.A., Kowal, A.S., Singer, M.A. & Lindquist, S. Protein disaggregation mediated by heat-shock protein Hsp104. Nature 372, 475\u2013478 (1994).","journal-title":"Nature"},{"key":"BFnchembio455_CR4","doi-asserted-by":"publisher","first-page":"169","DOI":"10.1038\/358169a0","volume":"358","author":"H Wiech","year":"1992","unstructured":"Wiech, H., Buchner, J., Zimmermann, R. & Jakob, U. Hsp90 chaperones protein folding in vitro. Nature 358, 169\u2013170 (1992).","journal-title":"Nature"},{"key":"BFnchembio455_CR5","doi-asserted-by":"publisher","first-page":"4137","DOI":"10.1002\/j.1460-2075.1993.tb06097.x","volume":"12","author":"H Schr\u00f6der","year":"1993","unstructured":"Schr\u00f6der, H., Langer, T., Hartl, F.U. & Bukau, B. DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage. EMBO J. 12, 4137\u20134144 (1993).","journal-title":"EMBO J."},{"key":"BFnchembio455_CR6","doi-asserted-by":"publisher","first-page":"620","DOI":"10.1038\/337620a0","volume":"337","author":"MY Cheng","year":"1989","unstructured":"Cheng, M.Y. et al. Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria. Nature 337, 620\u2013625 (1989).","journal-title":"Nature"},{"key":"BFnchembio455_CR7","doi-asserted-by":"publisher","first-page":"884","DOI":"10.1038\/342884a0","volume":"342","author":"P Goloubinoff","year":"1989","unstructured":"Goloubinoff, P., Christeller, J.T., Gatenby, A.A. & Lorimer, G.H. Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and Mg-ATP. Nature 342, 884\u2013889 (1989).","journal-title":"Nature"},{"key":"BFnchembio455_CR8","doi-asserted-by":"crossref","first-page":"1517","DOI":"10.1016\/S0021-9258(18)53882-5","volume":"268","author":"U Jakob","year":"1993","unstructured":"Jakob, U., Gaestel, M., Engel, K. & Buchner, J. Small heat shock proteins are molecular chaperones. J. Biol. Chem. 268, 1517\u20131520 (1993).","journal-title":"J. Biol. Chem."},{"key":"BFnchembio455_CR9","doi-asserted-by":"publisher","first-page":"614","DOI":"10.1038\/371614a0","volume":"371","author":"WA Fenton","year":"1994","unstructured":"Fenton, W.A., Kashi, Y., Furtak, K. & Horwich, A.L. Residues in chaperonin GroEL required for polypeptide binding and release. Nature 371, 614\u2013619 (1994).","journal-title":"Nature"},{"key":"BFnchembio455_CR10","doi-asserted-by":"publisher","first-page":"1501","DOI":"10.1093\/emboj\/16.7.1501","volume":"16","author":"S R\u00fcdiger","year":"1997","unstructured":"R\u00fcdiger, S., Germeroth, L., Schneider-Mergener, J. & Bukau, B. Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries. EMBO J. 16, 1501\u20131507 (1997).","journal-title":"EMBO J."},{"key":"BFnchembio455_CR11","doi-asserted-by":"publisher","first-page":"1042","DOI":"10.1093\/emboj\/20.5.1042","volume":"20","author":"S R\u00fcdiger","year":"2001","unstructured":"R\u00fcdiger, S., Schneider-Mergener, J. & Bukau, B. Its substrate specificity characterizes the DnaJ co-chaperone as a scanning factor for the DnaK chaperone. EMBO J. 20, 1042\u20131050 (2001).","journal-title":"EMBO J."},{"key":"BFnchembio455_CR12","doi-asserted-by":"publisher","first-page":"1852","DOI":"10.1126\/science.1068408","volume":"295","author":"FU Hartl","year":"2002","unstructured":"Hartl, F.U. & Hayer-Hartl, M. Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 295, 1852\u20131858 (2002).","journal-title":"Science"},{"key":"BFnchembio455_CR13","doi-asserted-by":"publisher","first-page":"249","DOI":"10.1385\/JMN:30:3:249","volume":"30","author":"MP Hinault","year":"2006","unstructured":"Hinault, M.P., Ben-Zvi, A. & Goloubinoff, P. Chaperones and proteases:cellular fold-controlling factors of proteins in neurodegenerative diseases and aging. J. Mol. Neurosci. 30, 249\u2013265 (2006).","journal-title":"J. Mol. Neurosci."},{"key":"BFnchembio455_CR14","doi-asserted-by":"publisher","first-page":"12021","DOI":"10.1073\/pnas.92.26.12021","volume":"92","author":"A Azem","year":"1995","unstructured":"Azem, A., Diamant, S., Kessel, M., Weiss, C. & Goloubinoff, P. The protein\u2014folding activity of chaperonins correlates with the symmetric GroEL14(GroES7)2 heterooligomer. Proc. Natl. Acad. Sci. USA 92, 12021\u201312025 (1995).","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"BFnchembio455_CR15","doi-asserted-by":"publisher","first-page":"273","DOI":"10.1021\/bi00001a033","volume":"34","author":"S Diamant","year":"1995","unstructured":"Diamant, S., Azem, A., Weiss, C. & Goloubinoff, P. Effect of free and ATP-bound magnesium and manganese ions on the ATPase activity of chaperonin GroEL14. Biochemistry 34, 273\u2013277 (1995).","journal-title":"Biochemistry"},{"key":"BFnchembio455_CR16","doi-asserted-by":"publisher","first-page":"36","DOI":"10.1038\/352036a0","volume":"352","author":"J Martin","year":"1991","unstructured":"Martin, J. et al. Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate. Nature 352, 36\u201342 (1991).","journal-title":"Nature"},{"key":"BFnchembio455_CR17","doi-asserted-by":"publisher","first-page":"37298","DOI":"10.1074\/jbc.M405627200","volume":"279","author":"A Ben-Zvi","year":"2004","unstructured":"Ben-Zvi, A., De los Rios, P., Dietler, G. & Goloubinoff, P. Active solubilization and refolding of stable protein aggregates by cooperative unfolding action of individual Hsp70 chaperones. J. Biol. Chem. 279, 37298\u201337303 (2004).","journal-title":"J. Biol. Chem."},{"key":"BFnchembio455_CR18","doi-asserted-by":"publisher","first-page":"21107","DOI":"10.1074\/jbc.M001293200","volume":"275","author":"S Diamant","year":"2000","unstructured":"Diamant, S., Ben-Zvi, A.P., Bukau, B. & Goloubinoff, P. Size-dependent disaggregation of stable protein aggregates by the DnaK chaperone machinery. J. Biol. Chem. 275, 21107\u201321113 (2000).","journal-title":"J. Biol. Chem."},{"key":"BFnchembio455_CR19","doi-asserted-by":"publisher","first-page":"9688","DOI":"10.1021\/bi980338u","volume":"37","author":"S Diamant","year":"1998","unstructured":"Diamant, S. & Goloubinoff, P. Temperature-controlled activity of DnaK-DnaJ-GrpE chaperones: Protein-folding arrest and recovery during and after heat shock depends on the substrate protein and the GrpE concentration. Biochemistry 37, 9688\u20139694 (1998).","journal-title":"Biochemistry"},{"key":"BFnchembio455_CR20","doi-asserted-by":"publisher","first-page":"939","DOI":"10.1016\/0092-8674(90)90268-J","volume":"62","author":"D Skowyra","year":"1990","unstructured":"Skowyra, D., Georgopoulos, C. & Zylicz, M. The E. coli dnaK gene product, the Hsp70 homolog, can reactivate heat-inactivated RNA polymerase in an ATP hydrolysis-dependent manner. Cell 62, 939\u2013944 (1990).","journal-title":"Cell"},{"key":"BFnchembio455_CR21","doi-asserted-by":"publisher","first-page":"11032","DOI":"10.1074\/jbc.273.18.11032","volume":"273","author":"L Veinger","year":"1998","unstructured":"Veinger, L., Diamant, S., Buchner, J. & Goloubinoff, P. The small heat-shock protein IbpB from Escherichia coli stabilizes stress-denatured proteins for subsequent refolding by a multichaperone network. J. Biol. Chem. 273, 11032\u201311037 (1998).","journal-title":"J. Biol. Chem."},{"key":"BFnchembio455_CR22","doi-asserted-by":"publisher","first-page":"232","DOI":"10.1016\/j.molcel.2008.05.006","volume":"31","author":"JP Schuermann","year":"2008","unstructured":"Schuermann, J.P. et al. Structure of the Hsp110: Hsc70 nucleotide exchange machine. Mol. Cell 31, 232\u2013243 (2008).","journal-title":"Mol. Cell"},{"key":"BFnchembio455_CR23","doi-asserted-by":"publisher","first-page":"73","DOI":"10.1016\/S0092-8674(00)81223-4","volume":"94","author":"JR Glover","year":"1998","unstructured":"Glover, J.R. & Lindquist, S. Hsp104, Hsp70, and Hsp40: A novel chaperone system that rescues previously aggregated proteins. Cell 94, 73\u201382 (1998).","journal-title":"Cell"},{"key":"BFnchembio455_CR24","doi-asserted-by":"publisher","first-page":"13732","DOI":"10.1073\/pnas.96.24.13732","volume":"96","author":"P Goloubinoff","year":"1999","unstructured":"Goloubinoff, P., Mogk, A., Ben Zvi, A.P., Tomoyasu, T. & Bukau, B. Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network. Proc. Natl. Acad. Sci. USA 96, 13732\u201313737 (1999).","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"BFnchembio455_CR25","doi-asserted-by":"publisher","first-page":"10345","DOI":"10.1073\/pnas.91.22.10345","volume":"91","author":"A Szabo","year":"1994","unstructured":"Szabo, A. et al. The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system DnaK, DnaJ, and GrpE. Proc. Natl. Acad. Sci. USA 91, 10345\u201310349 (1994).","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"BFnchembio455_CR26","doi-asserted-by":"publisher","first-page":"28387","DOI":"10.1074\/jbc.270.47.28387","volume":"270","author":"S Diamant","year":"1995","unstructured":"Diamant, S., Azem, A., Weiss, C. & Goloubinoff, P. Increased efficiency of GroE-assisted protein-folding by manganese ions. J. Biol. Chem. 270, 28387\u201328391 (1995).","journal-title":"J. Biol. Chem."},{"key":"BFnchembio455_CR27","doi-asserted-by":"publisher","first-page":"432","DOI":"10.2174\/138920309789351930","volume":"10","author":"SK Sharma","year":"2009","unstructured":"Sharma, S.K., Christen, P. & Goloubinoff, P. Disaggregating chaperones: An unfolding story. Curr. Protein Pept. Sci. 10, 432\u2013446 (2009).","journal-title":"Curr. Protein Pept. Sci."},{"key":"BFnchembio455_CR28","doi-asserted-by":"publisher","first-page":"6166","DOI":"10.1073\/pnas.0510496103","volume":"103","author":"P De Los Rios","year":"2006","unstructured":"De Los Rios, P., Ben-Zvi, A., Slutsky, O., Azem, A. & Goloubinoff, P. Hsp70 chaperones accelerate protein translocation and the unfolding of stable protein aggregates by entropic pulling. Proc. Natl. Acad. Sci. USA 103, 6166\u20136171 (2006).","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"BFnchembio455_CR29","doi-asserted-by":"publisher","first-page":"86","DOI":"10.1134\/S0026893307010128","volume":"41","author":"MS Svetlov","year":"2007","unstructured":"Svetlov, M.S., Kolb, V.A. & Spirin, A.S. Folding of the firefly luciferase polypeptide chain with the immobilized C terminus. Mol. Biol. 41, 86\u201392 (2007).","journal-title":"Mol. Biol."},{"key":"BFnchembio455_CR30","doi-asserted-by":"publisher","first-page":"287","DOI":"10.1016\/S0969-2126(96)00033-0","volume":"4","author":"E Conti","year":"1996","unstructured":"Conti, E., Franks, N.P. & Brick, P. Crystal structure of firefly luciferase throws light on a superfamily of adenylate-forming enzymes. Structure 4, 287\u2013298 (1996).","journal-title":"Structure"},{"key":"BFnchembio455_CR31","doi-asserted-by":"crossref","unstructured":"Fishbein, W.N. & Winkert, J.W. in Proteins at Low Temperatures, Vol. 180 (ed. Fennema, O.) 55\u201382 (American Chemical Society, 1979).","DOI":"10.1021\/ba-1979-0180.ch004"},{"key":"BFnchembio455_CR32","doi-asserted-by":"publisher","first-page":"4303","DOI":"10.1021\/bi962727z","volume":"36","author":"W Barouch","year":"1997","unstructured":"Barouch, W., Prasad, K., Greene, L. & Eisenberg, E. Auxilin-induced interaction of the molecular chaperone Hsc70 with clathrin baskets. Biochemistry 36, 4303\u20134308 (1997).","journal-title":"Biochemistry"},{"key":"BFnchembio455_CR33","doi-asserted-by":"publisher","first-page":"19038","DOI":"10.1074\/jbc.M300756200","volume":"278","author":"W Han","year":"2003","unstructured":"Han, W. & Christen, P. Mechanism of the targeting action of DnaJ in the DnaK molecular chaperone system. J. Biol. Chem. 278, 19038\u201319043 (2003).","journal-title":"J. Biol. Chem."},{"key":"BFnchembio455_CR34","doi-asserted-by":"publisher","first-page":"5452","DOI":"10.1073\/pnas.96.10.5452","volume":"96","author":"T Laufen","year":"1999","unstructured":"Laufen, T. et al. Mechanism of regulation of Hsp70 chaperones by DnaJ cochaperones. Proc. Natl. Acad. Sci. USA 96, 5452\u20135457 (1999).","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"BFnchembio455_CR35","doi-asserted-by":"publisher","first-page":"27957","DOI":"10.1074\/jbc.M403558200","volume":"279","author":"D Brehmer","year":"2004","unstructured":"Brehmer, D., Gassler, C., Rist, W., Mayer, M.P. & Bukau, B. Influence of GrpE on DnaK-substrate interactions. J. Biol. Chem. 279, 27957\u201327964 (2004).","journal-title":"J. Biol. Chem."},{"key":"BFnchembio455_CR36","doi-asserted-by":"publisher","first-page":"254","DOI":"10.1038\/85002","volume":"8","author":"A Mally","year":"2001","unstructured":"Mally, A. & Witt, S.N. GrpE accelerates peptide binding and release from the high affinity state of DnaK. Nat. Struct. Biol. 8, 254\u2013257 (2001).","journal-title":"Nat. Struct. Biol."},{"key":"BFnchembio455_CR37","doi-asserted-by":"publisher","first-page":"496","DOI":"10.1529\/biophysj.106.083394","volume":"91","author":"B Hu","year":"2006","unstructured":"Hu, B., Mayer, M.P. & Tomita, M. Modeling Hsp70-mediated protein folding. Biophys. J. 91, 496\u2013507 (2006).","journal-title":"Biophys. J."},{"key":"BFnchembio455_CR38","doi-asserted-by":"publisher","first-page":"586","DOI":"10.1038\/76819","volume":"7","author":"MP Mayer","year":"2000","unstructured":"Mayer, M.P. et al. Multistep mechanism of substrate binding determines chaperone activity of Hsp70. Nat. Struct. Biol. 7, 586\u2013593 (2000).","journal-title":"Nat. Struct. Biol."},{"key":"BFnchembio455_CR39","doi-asserted-by":"publisher","first-page":"1039","DOI":"10.1016\/j.jmb.2005.02.026","volume":"347","author":"S Popp","year":"2005","unstructured":"Popp, S. et al. Structural dynamics of the DnaK-peptide complex. J. Mol. Biol. 347, 1039\u20131052 (2005).","journal-title":"J. Mol. Biol."},{"key":"BFnchembio455_CR40","doi-asserted-by":"publisher","first-page":"8471","DOI":"10.1073\/pnas.0903503106","volume":"106","author":"EB Bertelsen","year":"2009","unstructured":"Bertelsen, E.B., Chang, L., Gestwicki, J.E. & Zuiderweg, E.R. Solution conformation of wild-type E. coli Hsp70 (DnaK) chaperone complexed with ADP and substrate. Proc. Natl. Acad. Sci. USA 106, 8471\u20138476 (2009).","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"BFnchembio455_CR41","doi-asserted-by":"publisher","first-page":"372","DOI":"10.1016\/j.tibs.2007.06.008","volume":"32","author":"P Goloubinoff","year":"2007","unstructured":"Goloubinoff, P. & De Los Rios, P. The mechanism of Hsp70 chaperones: (entropic) pulling the models together. Trends Biochem. Sci. 32, 372\u2013380 (2007).","journal-title":"Trends Biochem. Sci."},{"key":"BFnchembio455_CR42","doi-asserted-by":"publisher","first-page":"833","DOI":"10.1016\/0092-8674(92)90294-M","volume":"69","author":"J Gamer","year":"1992","unstructured":"Gamer, J., Bujard, H. & Bukau, B. Physical interaction between heat shock proteins DnaK, DnaJ, and GrpE and the bacterial heat shock transcription factor sigma 32. Cell 69, 833\u2013842 (1992).","journal-title":"Cell"},{"key":"BFnchembio455_CR43","doi-asserted-by":"publisher","first-page":"347","DOI":"10.1016\/j.molcel.2008.09.016","volume":"32","author":"F Rodriguez","year":"2008","unstructured":"Rodriguez, F. et al. Molecular basis for regulation of the heat shock transcription factor sigma32 by the DnaK and DnaJ chaperones. Mol. Cell 32, 347\u2013358 (2008).","journal-title":"Mol. Cell"},{"key":"BFnchembio455_CR44","doi-asserted-by":"publisher","first-page":"11","DOI":"10.1038\/nrn1587","volume":"6","author":"PJ Muchowski","year":"2005","unstructured":"Muchowski, P.J. & Wacker, J.L. Modulation of neurodegeneration by molecular chaperones. Nat. Rev. Neurosci. 6, 11\u201322 (2005).","journal-title":"Nat. Rev. Neurosci."},{"key":"BFnchembio455_CR45","doi-asserted-by":"publisher","first-page":"318","DOI":"10.1111\/j.1432-1033.1996.0318n.x","volume":"237","author":"B Feifel","year":"1996","unstructured":"Feifel, B., Sandmeier, E., Schonfeld, H.J. & Christen, P. Potassium ions and the molecular-chaperone activity of DnaK. Eur. J. Biochem. 237, 318\u2013321 (1996).","journal-title":"Eur. J. Biochem."},{"key":"BFnchembio455_CR46","doi-asserted-by":"publisher","first-page":"5030","DOI":"10.1128\/jb.172.9.5030-5034.1990","volume":"172","author":"H Hellebust","year":"1990","unstructured":"Hellebust, H., Uhlen, M. & Enfors, S.O. Interaction between heat-shock protein Dnak and recombinant staphylococcal protein-A. J. Bacteriol. 172, 5030\u20135034 (1990).","journal-title":"J. Bacteriol."},{"key":"BFnchembio455_CR47","doi-asserted-by":"publisher","first-page":"2183","DOI":"10.1074\/jbc.270.5.2183","volume":"270","author":"HJ Sch\u00f6nfeld","year":"1995","unstructured":"Sch\u00f6nfeld, H.J., Schmidt, D., Schroder, H. & Bukau, B. The Dnak chaperone system of Escherichia coli\u2014quaternary structures and interactions of the Dnak and Grpe components. J. Biol. Chem. 270, 2183\u20132189 (1995).","journal-title":"J. Biol. Chem."},{"key":"BFnchembio455_CR48","doi-asserted-by":"publisher","first-page":"19044","DOI":"10.1074\/jbc.M300922200","volume":"278","author":"P Bischofberger","year":"2003","unstructured":"Bischofberger, P., Han, W.J., Feifel, B., Schonfeld, H.J. & Christen, P. D-Peptides as inhibitors of the DnaK\/DnaJ\/GrpE chaperone system. J. Biol. Chem. 278, 19044\u201319047 (2003).","journal-title":"J. Biol. Chem."}],"container-title":["Nature Chemical Biology"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/www.nature.com\/articles\/nchembio.455.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/www.nature.com\/articles\/nchembio.455","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/www.nature.com\/articles\/nchembio.455.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,5,18]],"date-time":"2023-05-18T15:49:02Z","timestamp":1684424942000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.nature.com\/articles\/nchembio.455"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2010,10,17]]},"references-count":48,"journal-issue":{"issue":"12","published-print":{"date-parts":[[2010,12]]}},"alternative-id":["BFnchembio455"],"URL":"https:\/\/doi.org\/10.1038\/nchembio.455","relation":{"has-review":[{"id-type":"doi","id":"10.3410\/f.6000960.6007063","asserted-by":"object"}]},"ISSN":["1552-4450","1552-4469"],"issn-type":[{"value":"1552-4450","type":"print"},{"value":"1552-4469","type":"electronic"}],"subject":[],"published":{"date-parts":[[2010,10,17]]}}}