{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,27]],"date-time":"2026-03-27T10:36:14Z","timestamp":1774607774316,"version":"3.50.1"},"reference-count":52,"publisher":"Springer Science and Business Media LLC","issue":"2","license":[{"start":{"date-parts":[[2010,12,19]],"date-time":"2010-12-19T00:00:00Z","timestamp":1292716800000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/www.springer.com\/tdm"},{"start":{"date-parts":[[2010,12,19]],"date-time":"2010-12-19T00:00:00Z","timestamp":1292716800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/www.springer.com\/tdm"}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Nature Chem"],"published-print":{"date-parts":[[2011,2]]},"DOI":"10.1038\/nchem.947","type":"journal-article","created":{"date-parts":[[2010,12,19]],"date-time":"2010-12-19T20:41:23Z","timestamp":1292791283000},"page":"126-132","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":242,"title":["Interrogating viral capsid assembly with ion mobility\u2013mass spectrometry"],"prefix":"10.1038","volume":"3","author":[{"given":"Charlotte","family":"Uetrecht","sequence":"first","affiliation":[]},{"given":"Ioana M.","family":"Barbu","sequence":"additional","affiliation":[]},{"given":"Glen K.","family":"Shoemaker","sequence":"additional","affiliation":[]},{"given":"Esther","family":"van Duijn","sequence":"additional","affiliation":[]},{"given":"Albert J. R.","family":"Heck","sequence":"additional","affiliation":[]}],"member":"297","published-online":{"date-parts":[[2010,12,19]]},"reference":[{"key":"BFnchem947_CR1","doi-asserted-by":"crossref","first-page":"291","DOI":"10.1016\/S0092-8674(00)80922-8","volume":"92","author":"B Alberts","year":"1998","unstructured":"Alberts, B. The cell as a collection of protein machines: preparing the next generation of molecular biologists. Cell 92, 291\u2013294 (1998).","journal-title":"Cell"},{"key":"BFnchem947_CR2","doi-asserted-by":"crossref","first-page":"973","DOI":"10.1038\/nature06523","volume":"450","author":"CV Robinson","year":"2007","unstructured":"Robinson, C. V., Sali, A. & Baumeister, W. The molecular sociology of the cell. Nature 450, 973\u2013982 (2007).","journal-title":"Nature"},{"key":"BFnchem947_CR3","doi-asserted-by":"crossref","first-page":"1452","DOI":"10.1021\/ja8055134","volume":"131","author":"E van Duijn","year":"2009","unstructured":"van Duijn, E., Barendregt, A., Synowsky, S., Versluis, C. & Heck, A. J. Chaperonin complexes monitored by ion mobility mass spectrometry. J. Am. Chem. Soc. 131, 1452\u20131459 (2009).","journal-title":"J. Am. Chem. Soc."},{"key":"BFnchem947_CR4","doi-asserted-by":"crossref","first-page":"197","DOI":"10.1146\/annurev.biophys.050708.133615","volume":"38","author":"MT Sykes","year":"2009","unstructured":"Sykes, M. T. & Williamson, J. R. A complex assembly landscape for the 30S ribosomal subunit. Annu. Rev. Biophys. 38, 197\u2013215 (2009).","journal-title":"Annu. Rev. Biophys."},{"key":"BFnchem947_CR5","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1016\/j.cell.2009.06.035","volume":"138","author":"HC Besche","year":"2009","unstructured":"Besche, H. C., Peth, A. & Goldberg, A. L. Getting to first base in proteasome assembly. Cell 138, 25\u201328 (2009).","journal-title":"Cell"},{"key":"BFnchem947_CR6","doi-asserted-by":"crossref","first-page":"18448","DOI":"10.1074\/jbc.M701534200","volume":"282","author":"M Sharon","year":"2007","unstructured":"Sharon, M., Witt, S., Glasmacher, E., Baumeister, W. & Robinson, C. V. Mass spectrometry reveals the missing links in the assembly pathway of the bacterial 20 S proteasome. J. Biol. Chem. 282, 18448\u201318457 (2007).","journal-title":"J. Biol. Chem."},{"key":"BFnchem947_CR7","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1101\/SQB.1962.027.001.005","volume":"27","author":"DL Caspar","year":"1962","unstructured":"Caspar, D. L. & Klug, A. Physical principles in the construction of regular viruses. Cold. Spring Harb. Symp. Quant. Biol. 27, 1\u201324 (1962).","journal-title":"Cold. Spring Harb. Symp. Quant. Biol."},{"key":"BFnchem947_CR8","doi-asserted-by":"crossref","first-page":"479","DOI":"10.1002\/jmr.754","volume":"18","author":"A Zlotnick","year":"2005","unstructured":"Zlotnick, A. Theoretical aspects of virus capsid assembly. J. Mol. Recogn. 18, 479\u2013490 (2005).","journal-title":"J. Mol. Recogn."},{"key":"BFnchem947_CR9","doi-asserted-by":"crossref","first-page":"541","DOI":"10.1016\/j.jmb.2007.03.020","volume":"369","author":"PG Stockley","year":"2007","unstructured":"Stockley, P. G. et al. A simple, RNA-mediated allosteric switch controls the pathway to formation of a T=3 viral capsid. J. Mol. Biol. 369, 541\u2013552 (2007).","journal-title":"J. Mol. Biol."},{"key":"BFnchem947_CR10","doi-asserted-by":"crossref","first-page":"287","DOI":"10.1126\/science.286.5438.287","volume":"286","author":"BV Prasad","year":"1999","unstructured":"Prasad, B. V. et al. X-ray crystallographic structure of the Norwalk virus capsid. Science 286, 287\u2013290 (1999).","journal-title":"Science"},{"key":"BFnchem947_CR11","doi-asserted-by":"crossref","first-page":"14644","DOI":"10.1021\/bi991611a","volume":"38","author":"A Zlotnick","year":"1999","unstructured":"Zlotnick, A., Johnson, J. M., Wingfield, P. W., Stahl, S. J. & Endres, D. A theoretical model successfully identifies features of hepatitis B virus capsid assembly. Biochemistry 38, 14644\u201314652 (1999).","journal-title":"Biochemistry"},{"key":"BFnchem947_CR12","doi-asserted-by":"crossref","first-page":"1776","DOI":"10.1056\/NEJMra0804575","volume":"361","author":"RI Glass","year":"2009","unstructured":"Glass, R. I., Parashar, U. D. & Estes, M. K. Norovirus gastroenteritis. N. Engl. J. Med. 361, 1776\u20131785 (2009).","journal-title":"N. Engl. J. Med."},{"key":"BFnchem947_CR13","doi-asserted-by":"crossref","first-page":"512","DOI":"10.1111\/j.1478-3231.2006.01269.x","volume":"26","author":"SK Sarin","year":"2006","unstructured":"Sarin, S. K. et al. Consensus on extra-hepatic portal vein obstruction. Liver Int. 26, 512\u2013519 (2006).","journal-title":"Liver Int."},{"key":"BFnchem947_CR14","first-page":"237","volume":"12(Suppl.),","author":"BV Prasad","year":"1996","unstructured":"Prasad, B. V., Hardy, M. E., Jiang, X. & Estes, M. K. Structure of Norwalk virus. Arch. Virol. 12(Suppl.), 237\u2013242 (1996).","journal-title":"Arch. Virol."},{"key":"BFnchem947_CR15","doi-asserted-by":"crossref","first-page":"771","DOI":"10.1016\/S1097-2765(01)80009-5","volume":"3","author":"SA Wynne","year":"1999","unstructured":"Wynne, S. A., Crowther, R. A. & Leslie, A. G. The crystal structure of the human hepatitis B virus capsid. Mol. Cell. 3, 771\u2013780 (1999).","journal-title":"Mol. Cell."},{"key":"BFnchem947_CR16","doi-asserted-by":"crossref","first-page":"943","DOI":"10.1016\/0092-8674(94)90142-2","volume":"77","author":"RA Crowther","year":"1994","unstructured":"Crowther, R. A. et al. Three-dimensional structure of hepatitis B virus core particles determined by electron cryomicroscopy. Cell 77, 943\u2013950 (1994).","journal-title":"Cell"},{"key":"BFnchem947_CR17","doi-asserted-by":"crossref","first-page":"405","DOI":"10.1128\/JVI.77.1.405-415.2003","volume":"77","author":"AM Hutson","year":"2003","unstructured":"Hutson, A. M., Atmar, R. L., Marcus, D. M. & Estes, M. K. Norwalk virus-like particle hemagglutination by binding to H histo-blood broup antigens. J. Virol. 77, 405\u2013415 (2003).","journal-title":"J. Virol."},{"key":"BFnchem947_CR18","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1016\/S0065-3527(05)64005-5","volume":"64","author":"AC Steven","year":"2005","unstructured":"Steven, A. C. et al. Structure, assembly, and antigenicity of hepatitis B virus capsid proteins. Adv. Virus Res. 64, 125\u2013164 (2005).","journal-title":"Adv. Virus Res."},{"key":"BFnchem947_CR19","doi-asserted-by":"crossref","first-page":"7412","DOI":"10.1021\/bi9604800","volume":"35","author":"A Zlotnick","year":"1996","unstructured":"Zlotnick, A. et al. Dimorphism of hepatitis B virus capsids is strongly influenced by the C-terminus of the capsid protein. Biochemistry 35, 7412\u20137421 (1996).","journal-title":"Biochemistry"},{"key":"BFnchem947_CR20","doi-asserted-by":"crossref","first-page":"9216","DOI":"10.1073\/pnas.0800406105","volume":"105","author":"C Uetrecht","year":"2008","unstructured":"Uetrecht, C. et al. High-resolution mass spectrometry of viral assemblies: molecular composition and stability of dimorphic hepatitis B virus capsids. Proc. Natl Acad. Sci. USA 105, 9216\u20139220 (2008).","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"BFnchem947_CR21","doi-asserted-by":"crossref","first-page":"843","DOI":"10.1016\/j.molcel.2006.04.025","volume":"22","author":"KA Dryden","year":"2006","unstructured":"Dryden, K. A. et al. Native hepatitis B virions and capsids visualized by electron cryomicroscopy. Mol. Cell. 22, 843\u2013850 (2006).","journal-title":"Mol. Cell."},{"key":"BFnchem947_CR22","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1111\/j.1574-6976.1995.tb00186.x","volume":"17","author":"RL Duda","year":"1995","unstructured":"Duda, R. L., Martincic, K., Xie, Z. & Hendrix, R. W. Bacteriophage HK97 head assembly. FEMS Microbiol. Rev. 17, 41\u201346 (1995).","journal-title":"FEMS Microbiol. Rev."},{"key":"BFnchem947_CR23","doi-asserted-by":"crossref","first-page":"11525","DOI":"10.1021\/bi0261645","volume":"41","author":"P Ceres","year":"2002","unstructured":"Ceres, P. & Zlotnick, A. Weak protein\u2013protein interactions are sufficient to drive assembly of hepatitis B virus capsids. Biochemistry 41, 11525\u201311531 (2002).","journal-title":"Biochemistry"},{"key":"BFnchem947_CR24","doi-asserted-by":"crossref","first-page":"927","DOI":"10.1038\/nmeth.1265","volume":"5","author":"AJ Heck","year":"2008","unstructured":"Heck, A. J. Native mass spectrometry: a bridge between interactomics and structural biology. Nat. Methods 5, 927\u2013933 (2008).","journal-title":"Nat. Methods"},{"key":"BFnchem947_CR25","doi-asserted-by":"crossref","first-page":"575","DOI":"10.1002\/mas.20176","volume":"27","author":"VL Morton","year":"2008","unstructured":"Morton, V. L., Stockley, P. G., Stonehouse, N. J. & Ashcroft, A. E. Insights into virus capsid assembly from non-covalent mass spectrometry. Mass Spectrom. Rev. 27, 575\u2013595 (2008).","journal-title":"Mass Spectrom. Rev."},{"key":"BFnchem947_CR26","doi-asserted-by":"crossref","first-page":"6247","DOI":"10.1002\/anie.200802410","volume":"47","author":"C Uetrecht","year":"2008","unstructured":"Uetrecht, C. et al. Stability and shape of hepatitis B virus capsids in vacuo. Angew. Chem. Int. Ed. Engl. 47, 6247\u20136251 (2008).","journal-title":"Angew. Chem. Int. Ed. Engl."},{"key":"BFnchem947_CR27","doi-asserted-by":"crossref","first-page":"1742","DOI":"10.1074\/mcp.M900620-MCP200","volume":"9","author":"GK Shoemaker","year":"2010","unstructured":"Shoemaker, G. K. et al. Norwalk virus assembly and stability monitored by mass spectrometry. Mol. Cell. Proteomics 9, 1742\u20131751 (2010).","journal-title":"Mol. Cell. Proteomics"},{"key":"BFnchem947_CR28","doi-asserted-by":"crossref","first-page":"1633","DOI":"10.1039\/B914002F","volume":"39","author":"C Uetrecht","year":"2010","unstructured":"Uetrecht, C., Rose, R. J., Duijn, E. V., Lorenzen, K. & Heck, A. J. R. Ion mobility mass spectrometry of proteins and protein assemblies. Chem. Soc. Rev. 39, 1633\u20131655 (2010).","journal-title":"Chem. Soc. Rev."},{"key":"BFnchem947_CR29","doi-asserted-by":"crossref","first-page":"385","DOI":"10.1016\/j.jmb.2008.02.017","volume":"379","author":"K Lorenzen","year":"2008","unstructured":"Lorenzen, K., Olia, A. S., Uetrecht, C., Cingolani, G. & Heck, A. J. Determination of stoichiometry and conformational changes in the first step of the P22 tail assembly. J. Mol. Biol. 379, 385\u2013396 (2008).","journal-title":"J. Mol. Biol."},{"key":"BFnchem947_CR30","doi-asserted-by":"crossref","first-page":"1658","DOI":"10.1126\/science.1120177","volume":"310","author":"BT Ruotolo","year":"2005","unstructured":"Ruotolo, B. T. et al. Evidence for macromolecular protein rings in the absence of bulk water. Science 310, 1658\u20131661 (2005).","journal-title":"Science"},{"key":"BFnchem947_CR31","doi-asserted-by":"crossref","first-page":"16082","DOI":"10.1021\/jp961623v","volume":"100","author":"MF Mesleh","year":"1996","unstructured":"Mesleh, M. F., Hunter, J. M., Shvartsburg, A. A., Schatz, G. C. & Jarrold, M. F. Structural information from ion mobility measurements: effects of the long-range potential. J. Phys. Chem. 100, 16082\u201316086 (1996).","journal-title":"J. Phys. Chem."},{"key":"BFnchem947_CR32","doi-asserted-by":"crossref","first-page":"86","DOI":"10.1016\/0009-2614(96)00941-4","volume":"261","author":"AA Shvartsburg","year":"1996","unstructured":"Shvartsburg, A. A. & Jarrold, M. F. An exact hard-spheres scattering model for the mobilities of polyatomic ions. Chem. Phys. Lett. 261, 86\u201391 (1996).","journal-title":"Chem. Phys. Lett."},{"key":"BFnchem947_CR33","doi-asserted-by":"crossref","first-page":"354","DOI":"10.1016\/j.ymeth.2004.03.024","volume":"34","author":"ZS Derewenda","year":"2004","unstructured":"Derewenda, Z. S. The use of recombinant methods and molecular engineering in protein crystallization. Methods 34, 354\u2013363 (2004).","journal-title":"Methods"},{"key":"BFnchem947_CR34","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1146\/annurev.physchem.51.1.179","volume":"51","author":"MF Jarrold","year":"2000","unstructured":"Jarrold, M. F. Peptides and proteins in the vapor phase. Annu. Rev. Phys. Chem. 51, 179\u2013207 (2000).","journal-title":"Annu. Rev. Phys. Chem."},{"key":"BFnchem947_CR35","doi-asserted-by":"crossref","first-page":"1607","DOI":"10.1128\/JVI.02033-09","volume":"84","author":"C Packianathan","year":"2010","unstructured":"Packianathan, C., Katen, S. P., Dann, C. E. III & Zlotnick, A. Conformational changes in the hepatitis B virus core protein are consistent with a role for allostery in virus assembly. J. Virol. 84, 1607\u20131615 (2010).","journal-title":"J. Virol."},{"key":"BFnchem947_CR36","doi-asserted-by":"crossref","first-page":"222","DOI":"10.1016\/j.virol.2006.02.038","volume":"349","author":"C Hsu","year":"2006","unstructured":"Hsu, C. et al. Characterization of polymorphism displayed by the coat protein mutants of tomato bushy stunt virus. Virology 349, 222\u2013229 (2006).","journal-title":"Virology"},{"key":"BFnchem947_CR37","doi-asserted-by":"crossref","first-page":"R157","DOI":"10.1016\/S0969-2126(00)00181-7","volume":"8","author":"T Dokland","year":"2000","unstructured":"Dokland, T. Freedom and restraint: themes in virus capsid assembly. Structure 8, R157\u2013R162 (2000).","journal-title":"Structure"},{"key":"BFnchem947_CR38","doi-asserted-by":"crossref","first-page":"581","DOI":"10.1016\/j.jmb.2007.10.044","volume":"375","author":"JK Hilmer","year":"2008","unstructured":"Hilmer, J. K., Zlotnick, A. & Bothner, B. Conformational equilibria and rates of localized motion within hepatitis B virus capsids. J. Mol. Biol. 375, 581\u2013594 (2008).","journal-title":"J. Mol. Biol."},{"key":"BFnchem947_CR39","doi-asserted-by":"crossref","first-page":"513","DOI":"10.1016\/j.jmb.2006.09.088","volume":"365","author":"KN Parent","year":"2007","unstructured":"Parent, K. N., Suhanovsky, M. M. & Teschke, C. M. Phage P22 procapsids equilibrate with free coat protein subunits. J. Mol. Biol. 365, 513\u2013522 (2007).","journal-title":"J. Mol. Biol."},{"key":"BFnchem947_CR40","doi-asserted-by":"crossref","first-page":"e1000563","DOI":"10.1371\/journal.ppat.1000563","volume":"5","author":"B Rabe","year":"2009","unstructured":"Rabe, B. et al. Nuclear entry of hepatitis B virus capsids involves disintegration to protein dimers followed by nuclear reassociation to capsids. PLoS Pathog. 5, e1000563 (2009).","journal-title":"PLoS Pathog."},{"key":"BFnchem947_CR41","doi-asserted-by":"crossref","first-page":"14","DOI":"10.1016\/j.jmb.2006.11.034","volume":"366","author":"A Zlotnick","year":"2007","unstructured":"Zlotnick, A. Distinguishing reversible from irreversible virus capsid assembly. J. Mol. Biol. 366, 14\u201318 (2007).","journal-title":"J. Mol. Biol."},{"key":"BFnchem947_CR42","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.ijms.2006.07.021","volume":"261","author":"SD Pringle","year":"2007","unstructured":"Pringle, S. D. et al. An investigation of the mobility separation of some peptide and protein ions using a new hybrid quadrupole\/travelling wave IMS\/oa-ToF instrument. Int. J. Mass Spectrom. 261, 1\u201312 (2007).","journal-title":"Int. J. Mass Spectrom."},{"key":"BFnchem947_CR43","doi-asserted-by":"crossref","first-page":"7473","DOI":"10.1021\/ac061039a","volume":"78","author":"RH van den Heuvel","year":"2006","unstructured":"van den Heuvel, R. H. et al. Improving the performance of a quadrupole time-of-flight instrument for macromolecular mass spectrometry. Anal. Chem. 78, 7473\u20137483 (2006).","journal-title":"Anal. Chem."},{"key":"BFnchem947_CR44","doi-asserted-by":"crossref","first-page":"4694","DOI":"10.1021\/ja056756l","volume":"128","author":"E van Duijn","year":"2006","unstructured":"van Duijn, E. et al. Tandem mass spectrometry of intact GroEL\u2013substrate complexes reveals substrate-specific conformational changes in the trans ring. J. Am. Chem. Soc. 128, 4694\u20134702 (2006).","journal-title":"J. Am. Chem. Soc."},{"key":"BFnchem947_CR45","doi-asserted-by":"crossref","first-page":"198","DOI":"10.1016\/j.ijms.2007.06.012","volume":"268","author":"K Lorenzen","year":"2007","unstructured":"Lorenzen, K., Versluis, C., van Duijn, E., van den Heuvel, R. H. H. & Heck, A. J. R. Optimizing macromolecular tandem mass spectrometry of large non-covalent complexes using heavy collision gases. Int. J. Mass Spectrom. 268, 198\u2013206 (2007).","journal-title":"Int. J. Mass Spectrom."},{"key":"BFnchem947_CR46","doi-asserted-by":"crossref","first-page":"1402","DOI":"10.1021\/ac0110552","volume":"74","author":"F Sobott","year":"2002","unstructured":"Sobott, F., Hernandez, H., McCammon, M. G., Tito, M. A. & Robinson, C. V. A tandem mass spectrometer for improved transmission and analysis of large macromolecular assemblies. Anal. Chem. 74, 1402\u20131407 (2002).","journal-title":"Anal. Chem."},{"key":"BFnchem947_CR47","doi-asserted-by":"crossref","first-page":"596","DOI":"10.1002\/rcm.275","volume":"15","author":"N Tahallah","year":"2001","unstructured":"Tahallah, N., Pinkse, M., Maier, C. S. & Heck, A. J. The effect of the source pressure on the abundance of ions of noncovalent protein assemblies in an electrospray ionization orthogonal time-of-flight instrument. Rapid Commun. Mass Spectrom. 15, 596\u2013601 (2001).","journal-title":"Rapid Commun. Mass Spectrom."},{"key":"BFnchem947_CR48","doi-asserted-by":"crossref","first-page":"6527","DOI":"10.1128\/JVI.66.11.6527-6532.1992","volume":"66","author":"X Jiang","year":"1992","unstructured":"Jiang, X., Wang, M., Graham, D. Y. & Estes, M. K. Expression, self-assembly, and antigenicity of the Norwalk virus capsid protein. J. Virol. 66, 6527\u20136532 (1992).","journal-title":"J. Virol."},{"key":"BFnchem947_CR49","doi-asserted-by":"crossref","first-page":"4919","DOI":"10.1021\/bi00015a003","volume":"34","author":"PT Wingfield","year":"1995","unstructured":"Wingfield, P. T., Stahl, S. J., Williams, R. W. & Steven, A. C. Hepatitis core antigen produced in Escherichia coli: subunit composition, conformational analysis, and in vitro capsid assembly. Biochemistry 34, 4919\u20134932 (1995).","journal-title":"Biochemistry"},{"key":"BFnchem947_CR50","doi-asserted-by":"crossref","first-page":"1139","DOI":"10.1038\/nprot.2008.78","volume":"3","author":"BT Ruotolo","year":"2008","unstructured":"Ruotolo, B. T., Benesch, J. L., Sandercock, A. M., Hyung, S. J. & Robinson, C. V. Ion mobility\u2013mass spectrometry analysis of large protein complexes. Nat. Protoc. 3, 1139\u20131152 (2008).","journal-title":"Nat. Protoc."},{"key":"BFnchem947_CR51","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1255\/ejms.947","volume":"15","author":"DP Smith","year":"2009","unstructured":"Smith, D. P. et al. Deciphering drift time measurements from travelling wave ion mobility spectrometry\u2013mass spectrometry studies. Eur. J. Mass Spectrom. 15, 113\u2013130 (2009).","journal-title":"Eur. J. Mass Spectrom."},{"key":"BFnchem947_CR52","doi-asserted-by":"crossref","first-page":"1175","DOI":"10.1016\/j.bpj.2010.05.033","volume":"99","author":"WH Roos","year":"2010","unstructured":"Roos, W. H. et al. Squeezing protein shells: how continuum elastic models, molecular dynamics simulations and experiments coalesce at the nanoscale. Biophys. J. 99, 1175\u20131181 (2010).","journal-title":"Biophys. J."}],"updated-by":[{"DOI":"10.1038\/nchem.2025","type":"erratum","label":"Erratum","source":"publisher","updated":{"date-parts":[[2014,7,23]],"date-time":"2014-07-23T00:00:00Z","timestamp":1406073600000}}],"container-title":["Nature Chemistry"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/www.nature.com\/articles\/nchem.947.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/www.nature.com\/articles\/nchem.947","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/www.nature.com\/articles\/nchem.947.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,5,18]],"date-time":"2023-05-18T19:29:57Z","timestamp":1684438197000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.nature.com\/articles\/nchem.947"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2010,12,19]]},"references-count":52,"journal-issue":{"issue":"2","published-print":{"date-parts":[[2011,2]]}},"alternative-id":["BFnchem947"],"URL":"https:\/\/doi.org\/10.1038\/nchem.947","relation":{"erratum":[{"id-type":"doi","id":"10.1038\/nchem.2025","asserted-by":"object"}]},"ISSN":["1755-4330","1755-4349"],"issn-type":[{"value":"1755-4330","type":"print"},{"value":"1755-4349","type":"electronic"}],"subject":[],"published":{"date-parts":[[2010,12,19]]},"assertion":[{"value":"9 September 2010","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"11 November 2010","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"19 December 2010","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"23 July 2014","order":4,"name":"change_date","label":"Change Date","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"Erratum","order":5,"name":"change_type","label":"Change Type","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"In the version of this Article originally published, the trace for cp4 was missing from Fig. 3a. This has now been corrected in the online versions of the Article.","order":6,"name":"change_details","label":"Change Details","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"The authors declare no competing financial interests.","order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Competing interests"}}]}}