{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,7]],"date-time":"2026-10-07T21:05:47Z","timestamp":1791407147621,"version":"4.3.3"},"reference-count":48,"publisher":"Springer Science and Business Media LLC","issue":"9","license":[{"start":{"date-parts":[[2013,8,4]],"date-time":"2013-08-04T00:00:00Z","timestamp":1375574400000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/www.springer.com\/tdm"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Nat Struct Mol Biol"],"published-print":{"date-parts":[[2013,9]]},"DOI":"10.1038\/nsmb.2639","type":"journal-article","created":{"date-parts":[[2013,8,4]],"date-time":"2013-08-04T19:28:29Z","timestamp":1375644509000},"page":"1069-1076","source":"Crossref","is-referenced-by-count":55,"title":["Dimeric WH2 domains in Vibrio\u00a0VopF promote actin filament barbed-end uncapping and assisted elongation"],"prefix":"10.1038","volume":"20","author":[{"given":"Julien","family":"Pernier","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jozsef","family":"Orban","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Balendu Sankara","family":"Avvaru","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Antoine","family":"J\u00e9gou","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Guillaume","family":"Romet-Lemonne","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"B\u00e9reng\u00e8re","family":"Guichard","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marie-France","family":"Carlier","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2013,8,4]]},"reference":[{"key":"BFnsmb2639_CR1","doi-asserted-by":"publisher","first-page":"310","DOI":"10.1016\/j.devcel.2009.08.012","volume":"17","author":"RH Insall","year":"2009","unstructured":"Insall, R.H. & Machesky, L.M. Actin dynamics at the leading edge: from simple machinery to complex networks. Dev. Cell 17, 310\u2013322 (2009).","journal-title":"Dev. Cell"},{"key":"BFnsmb2639_CR2","doi-asserted-by":"publisher","first-page":"449","DOI":"10.1146\/annurev-biophys-051309-103849","volume":"39","author":"B Bugyi","year":"2010","unstructured":"Bugyi, B. & Carlier, M.F. Control of actin filament treadmilling in cell motility. Annu. Rev. Biophys. 39, 449\u2013470 (2010).","journal-title":"Annu. Rev. Biophys."},{"key":"BFnsmb2639_CR3","doi-asserted-by":"publisher","first-page":"569","DOI":"10.1016\/j.ceb.2011.07.003","volume":"23","author":"K Rottner","year":"2011","unstructured":"Rottner, K. & Stradal, T.E. Actin dynamics and turnover in cell motility. Curr. Opin. Cell Biol. 23, 569\u2013578 (2011).","journal-title":"Curr. Opin. Cell Biol."},{"key":"BFnsmb2639_CR4","doi-asserted-by":"publisher","first-page":"2390","DOI":"10.1111\/j.1742-4658.2010.07653.x","volume":"277","author":"KG Campellone","year":"2010","unstructured":"Campellone, K.G. Cytoskeleton-modulating effectors of enteropathogenic and enterohaemorrhagic Escherichia coli: Tir, EspFU and actin pedestal assembly. FEBS J. 277, 2390\u20132402 (2010).","journal-title":"FEBS J."},{"key":"BFnsmb2639_CR5","doi-asserted-by":"publisher","first-page":"7","DOI":"10.1083\/jcb.201103148","volume":"195","author":"CM Haglund","year":"2011","unstructured":"Haglund, C.M. & Welch, M.D. Pathogens and polymers: microbe-host interactions illuminate the cytoskeleton. J. Cell Biol. 195, 7\u201317 (2011).","journal-title":"J. Cell Biol."},{"key":"BFnsmb2639_CR6","doi-asserted-by":"publisher","first-page":"536","DOI":"10.1016\/j.chom.2009.10.011","volume":"6","author":"MP Dodding","year":"2009","unstructured":"Dodding, M.P. & Way, M. Nck- and N-WASP-dependent actin-based motility is conserved in divergent vertebrate poxviruses. Cell Host Microbe 6, 536\u2013550 (2009).","journal-title":"Cell Host Microbe"},{"key":"BFnsmb2639_CR7","doi-asserted-by":"publisher","first-page":"1057","DOI":"10.1038\/ncb2109","volume":"12","author":"CM Haglund","year":"2010","unstructured":"Haglund, C.M., Choe, J.E., Skau, C.T., Kovar, D.R. & Welch, M.D. Rickettsia Sca2 is a bacterial formin-like mediator of actin-based motility. Nat. Cell Biol. 12, 1057\u20131063 (2010).","journal-title":"Nat. Cell Biol."},{"key":"BFnsmb2639_CR8","doi-asserted-by":"publisher","first-page":"95","DOI":"10.1016\/j.chom.2007.03.005","volume":"1","author":"VC Tam","year":"2007","unstructured":"Tam, V.C., Serruto, D., Dziejman, M., Brieher, W. & Mekalanos, J.J. A type III secretion system in Vibrio cholerae translocates a formin\/spire hybrid-like actin nucleator to promote intestinal colonization. Cell Host Microbe 1, 95\u2013107 (2007).","journal-title":"Cell Host Microbe"},{"key":"BFnsmb2639_CR9","doi-asserted-by":"publisher","first-page":"17117","DOI":"10.1073\/pnas.0703196104","volume":"104","author":"AD Liverman","year":"2007","unstructured":"Liverman, A.D. et al. Arp2\/3-independent assembly of actin by Vibrio type III effector VopL. Proc. Natl. Acad. Sci. USA 104, 17117\u201317122 (2007).","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"BFnsmb2639_CR10","doi-asserted-by":"publisher","first-page":"650","DOI":"10.1016\/j.tcb.2010.08.014","volume":"20","author":"K Rottner","year":"2010","unstructured":"Rottner, K., H\u00e4nisch, J. & Campellone, K.G. WASH, WHAMM and JMY: regulation of Arp2\/3 complex and beyond. Trends Cell Biol. 20, 650\u2013661 (2010).","journal-title":"Trends Cell Biol."},{"key":"BFnsmb2639_CR11","doi-asserted-by":"crossref","first-page":"5267","DOI":"10.1242\/dev.126.23.5267","volume":"126","author":"A Wellington","year":"1999","unstructured":"Wellington, A. et al. Spire contains actin binding domains and is related to ascidian posterior end mark-5. Development 126, 5267\u20135274 (1999).","journal-title":"Development"},{"key":"BFnsmb2639_CR12","doi-asserted-by":"publisher","first-page":"16","DOI":"10.1016\/S0012-1606(03)00323-3","volume":"262","author":"EA Carroll","year":"2003","unstructured":"Carroll, E.A. et al. Cordon-bleu is a conserved gene involved in neural tube formation. Dev. Biol. 262, 16\u201331 (2003).","journal-title":"Dev. Biol."},{"key":"BFnsmb2639_CR13","doi-asserted-by":"publisher","first-page":"92","DOI":"10.1016\/S0014-5793(01)03242-2","volume":"513","author":"E Paunola","year":"2002","unstructured":"Paunola, E., Mattila, P.K. & Lappalainen, P. WH2 domain: a small, versatile adapter for actin monomers. FEBS Lett. 513, 92\u201397 (2002).","journal-title":"FEBS Lett."},{"key":"BFnsmb2639_CR14","doi-asserted-by":"publisher","first-page":"351","DOI":"10.3109\/10409230903277340","volume":"44","author":"R Dominguez","year":"2009","unstructured":"Dominguez, R. Actin filament nucleation and elongation factors\u2013structure-function relationships. Crit. Rev. Biochem. Mol. Biol. 44, 351\u2013366 (2009).","journal-title":"Crit. Rev. Biochem. Mol. Biol."},{"key":"BFnsmb2639_CR15","doi-asserted-by":"publisher","first-page":"55","DOI":"10.1016\/B978-0-12-386037-8.00005-3","volume":"290","author":"MF Carlier","year":"2011","unstructured":"Carlier, M.F., Husson, C., Renault, L. & Didry, D. Control of actin assembly by the WH2 domains and their multifunctional tandem repeats in Spire and Cordon-Bleu. Int. Rev. Cell. Mol. Biol. 290, 55\u201385 (2011).","journal-title":"Int. Rev. Cell. Mol. Biol."},{"key":"BFnsmb2639_CR16","doi-asserted-by":"publisher","first-page":"382","DOI":"10.1038\/nature03241","volume":"433","author":"ME Quinlan","year":"2005","unstructured":"Quinlan, M.E., Heuser, J.E., Kerkhoff, E. & Mullins, R.D. Drosophila Spire is an actin nucleation factor. Nature 433, 382\u2013388 (2005).","journal-title":"Nature"},{"key":"BFnsmb2639_CR17","doi-asserted-by":"publisher","first-page":"337","DOI":"10.1016\/j.cell.2007.08.030","volume":"131","author":"R Ahuja","year":"2007","unstructured":"Ahuja, R. et al. Cordon-bleu is an actin nucleation factor and controls neuronal morphology. Cell 131, 337\u2013350 (2007).","journal-title":"Cell"},{"key":"BFnsmb2639_CR18","doi-asserted-by":"publisher","first-page":"555","DOI":"10.1016\/j.molcel.2007.09.018","volume":"28","author":"M Bosch","year":"2007","unstructured":"Bosch, M. et al. Analysis of the function of Spire in actin assembly and its synergy with formin and profilin. Mol. Cell 28, 555\u2013568 (2007).","journal-title":"Mol. Cell"},{"key":"BFnsmb2639_CR19","doi-asserted-by":"publisher","first-page":"464","DOI":"10.1016\/j.molcel.2011.07.010","volume":"43","author":"C Husson","year":"2011","unstructured":"Husson, C., Renault, L., Didry, D., Pantaloni, D. & Carlier, M.F. Cordon-Bleu uses WH2 domains as multifunctional dynamizers of actin filament assembly. Mol. Cell 43, 464\u2013477 (2011).","journal-title":"Mol. Cell"},{"key":"BFnsmb2639_CR20","doi-asserted-by":"publisher","first-page":"1060","DOI":"10.1038\/nsmb.2109","volume":"18","author":"S Namgoong","year":"2011","unstructured":"Namgoong, S. et al. Mechanism of actin filament nucleation by Vibrio VopL and implications for tandem W domain nucleation. Nat. Struct. Mol. Biol. 18, 1060\u20131067 (2011).","journal-title":"Nat. Struct. Mol. Biol."},{"key":"BFnsmb2639_CR21","doi-asserted-by":"publisher","first-page":"1068","DOI":"10.1038\/nsmb.2110","volume":"18","author":"B Yu","year":"2011","unstructured":"Yu, B., Cheng, H.C., Brautigam, C.A., Tomchick, D.R. & Rosen, M.K. Mechanism of actin filament nucleation by the bacterial effector VopL. Nat. Struct. Mol. Biol. 18, 1068\u20131074 (2011).","journal-title":"Nat. Struct. Mol. Biol."},{"key":"BFnsmb2639_CR22","doi-asserted-by":"publisher","first-page":"967","DOI":"10.1038\/nsmb.2130","volume":"18","author":"MF Carlier","year":"2011","unstructured":"Carlier, M.F. A new twist in actin filament nucleation. Nat. Struct. Mol. Biol. 18, 967\u2013969 (2011).","journal-title":"Nat. Struct. Mol. Biol."},{"key":"BFnsmb2639_CR23","doi-asserted-by":"publisher","first-page":"201","DOI":"10.1002\/j.1460-2075.1996.tb00350.x","volume":"15","author":"M Van Troys","year":"1996","unstructured":"Van Troys, M. et al. The actin binding site of thymosin \u03b24 mapped by mutational analysis. EMBO J. 15, 201\u2013210 (1996).","journal-title":"EMBO J."},{"key":"BFnsmb2639_CR24","doi-asserted-by":"publisher","first-page":"901","DOI":"10.1016\/j.cell.2006.12.049","volume":"128","author":"C Co","year":"2007","unstructured":"Co, C., Wong, D.T., Gierke, S., Chang, V. & Taunton, J. Mechanism of actin network attachment to moving membranes: barbed end capture by N-WASP WH2 domains. Cell 128, 901\u2013913 (2007).","journal-title":"Cell"},{"key":"BFnsmb2639_CR25","doi-asserted-by":"publisher","first-page":"6599","DOI":"10.1073\/pnas.81.21.6599","volume":"81","author":"M Elzinga","year":"1984","unstructured":"Elzinga, M. & Phelan, J.J. F-actin is intermolecularly crosslinked by N,N\u2032-p-phenylenedimaleimide through lysine-191 and cysteine-374. Proc. Natl. Acad. Sci. USA 81, 6599\u20136602 (1984).","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"BFnsmb2639_CR26","doi-asserted-by":"publisher","first-page":"2516","DOI":"10.1016\/S0006-3495(00)76797-X","volume":"78","author":"EM De La Cruz","year":"2000","unstructured":"De La Cruz, E.M. et al. Thymosin-\u03b24 changes the conformation and dynamics of actin monomers. Biophys. J. 78, 2516\u20132527 (2000).","journal-title":"Biophys. J."},{"key":"BFnsmb2639_CR27","doi-asserted-by":"publisher","first-page":"611","DOI":"10.1016\/S0092-8674(04)00403-9","volume":"117","author":"M Hertzog","year":"2004","unstructured":"Hertzog, M. et al. The \u03b2-thymosin\/WH2 domain; structural basis for the switch from inhibition to promotion of actin assembly. Cell 117, 611\u2013623 (2004).","journal-title":"Cell"},{"key":"BFnsmb2639_CR28","doi-asserted-by":"publisher","first-page":"183","DOI":"10.1016\/S1937-6448(08)00604-7","volume":"267","author":"JA Cooper","year":"2008","unstructured":"Cooper, J.A. & Sept, D. New insights into mechanism and regulation of actin capping protein. Int. Rev. Cell. Mol. Biol. 267, 183\u2013206 (2008).","journal-title":"Int. Rev. Cell. Mol. Biol."},{"key":"BFnsmb2639_CR29","doi-asserted-by":"publisher","first-page":"5626","DOI":"10.1038\/sj.emboj.7601395","volume":"25","author":"A Narita","year":"2006","unstructured":"Narita, A., Takeda, S., Yamashita, A. & Ma\u00e9da, Y. Structural basis of actin filament capping at the barbed-end: a cryo-electron microscopy study. EMBO J. 25, 5626\u20135633 (2006).","journal-title":"EMBO J."},{"key":"BFnsmb2639_CR30","doi-asserted-by":"publisher","first-page":"794","DOI":"10.1016\/j.jmb.2010.10.017","volume":"404","author":"T Kim","year":"2010","unstructured":"Kim, T., Cooper, J.A. & Sept, D. The interaction of capping protein with the barbed end of the actin filament. J. Mol. Biol. 404, 794\u2013802 (2010).","journal-title":"J. Mol. Biol."},{"key":"BFnsmb2639_CR31","doi-asserted-by":"publisher","first-page":"1531","DOI":"10.1016\/S0960-9822(03)00559-1","volume":"13","author":"MA Wear","year":"2003","unstructured":"Wear, M.A., Yamashita, A., Kim, K., Ma\u00e9da, Y. & Cooper, J.A. How capping protein binds the barbed end of the actin filament. Curr. Biol. 13, 1531\u20131537 (2003).","journal-title":"Curr. Biol."},{"key":"BFnsmb2639_CR32","doi-asserted-by":"publisher","first-page":"2707","DOI":"10.1074\/jbc.M109.031203","volume":"285","author":"I Fujiwara","year":"2010","unstructured":"Fujiwara, I., Remmert, K. & Hammer, J.A. III. Direct observation of the uncapping of capping protein-capped actin filaments by CARMIL homology domain 3. J. Biol. Chem. 285, 2707\u20132720 (2010).","journal-title":"J. Biol. Chem."},{"key":"BFnsmb2639_CR33","doi-asserted-by":"publisher","first-page":"e1001161","DOI":"10.1371\/journal.pbio.1001161","volume":"9","author":"A J\u00e9gou","year":"2011","unstructured":"J\u00e9gou, A. et al. Individual actin filaments in a microfluidic flow reveal the mechanism of ATP hydrolysis and give insight into the properties of profilin. PLoS Biol. 9, e1001161 (2011).","journal-title":"PLoS Biol."},{"key":"BFnsmb2639_CR34","doi-asserted-by":"publisher","first-page":"441","DOI":"10.1038\/nature07685","volume":"457","author":"T Oda","year":"2009","unstructured":"Oda, T., Iwasa, M., Aihara, T., Ma\u00e9da, Y. & Narita, A. The nature of the globular- to fibrous-actin transition. Nature 457, 441\u2013445 (2009).","journal-title":"Nature"},{"key":"BFnsmb2639_CR35","doi-asserted-by":"publisher","first-page":"1529","DOI":"10.1093\/emboj\/cdg167","volume":"22","author":"A Yamashita","year":"2003","unstructured":"Yamashita, A., Maeda, K. & Ma\u00e9da, Y. Crystal structure of CapZ: structural basis for actin filament barbed end capping. EMBO J. 22, 1529\u20131538 (2003).","journal-title":"EMBO J."},{"key":"BFnsmb2639_CR36","doi-asserted-by":"publisher","first-page":"1334","DOI":"10.1126\/science.1229091","volume":"338","author":"P Gayathri","year":"2012","unstructured":"Gayathri, P. et al. A bipolar spindle of antiparallel ParM Filaments drives bacterial plasmid segregation. Science 338, 1334\u20131337 (2012).","journal-title":"Science"},{"key":"BFnsmb2639_CR37","doi-asserted-by":"publisher","first-page":"16644","DOI":"10.1073\/pnas.0507021102","volume":"102","author":"D Chereau","year":"2005","unstructured":"Chereau, D. et al. Actin-bound structures of Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 and the implications for filament assembly. Proc. Natl. Acad. Sci. USA 102, 16644\u201316649 (2005).","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"BFnsmb2639_CR38","doi-asserted-by":"publisher","first-page":"2943","DOI":"10.1038\/emboj.2008.211","volume":"27","author":"D Breitsprecher","year":"2008","unstructured":"Breitsprecher, D. et al. Clustering of VASP actively drives processive, WH2 domain-mediated actin filament elongation. EMBO J. 27, 2943\u20132954 (2008).","journal-title":"EMBO J."},{"key":"BFnsmb2639_CR39","doi-asserted-by":"publisher","first-page":"571","DOI":"10.1083\/jcb.201003014","volume":"191","author":"SD Hansen","year":"2010","unstructured":"Hansen, S.D. & Mullins, R.D. VASP is a processive actin polymerase that requires monomeric actin for barbed end association. J. Cell Biol. 191, 571\u2013584 (2010).","journal-title":"J. Cell Biol."},{"key":"BFnsmb2639_CR40","doi-asserted-by":"publisher","first-page":"116","DOI":"10.1016\/j.gene.2013.04.071","volume":"525","author":"R Tripathi","year":"2013","unstructured":"Tripathi, R., Kaithwas, V., Dureja, C. & Raychaudhuri, S. Alanine-scanning mutagenesis of WH2 domains of VopF reveals residues important for conferring lethality in a Saccharomyces cerevisiae model. Gene 525, 116\u2013123 (2013).","journal-title":"Gene"},{"key":"BFnsmb2639_CR41","doi-asserted-by":"publisher","first-page":"667","DOI":"10.1016\/S0006-3495(01)75731-1","volume":"81","author":"D Sept","year":"2001","unstructured":"Sept, D. & McCammon, J.A. Thermodynamics and kinetics of actin filament nucleation. Biophys. J. 81, 667\u2013674 (2001).","journal-title":"Biophys. J."},{"key":"BFnsmb2639_CR42","doi-asserted-by":"publisher","first-page":"387","DOI":"10.1083\/jcb.200207148","volume":"160","author":"S Wiesner","year":"2003","unstructured":"Wiesner, S. et al. A biomimetic motility assay provides insight into the mechanism of actin-based motility. J. Cell Biol. 160, 387\u2013398 (2003).","journal-title":"J. Cell Biol."},{"key":"BFnsmb2639_CR43","doi-asserted-by":"publisher","first-page":"363","DOI":"10.1016\/j.cell.2004.07.019","volume":"118","author":"MR Mejillano","year":"2004","unstructured":"Mejillano, M.R. et al. Lamellipodial versus filopodial mode of the actin nanomachinery: pivotal role of the filament barbed end. Cell 118, 363\u2013373 (2004).","journal-title":"Cell"},{"key":"BFnsmb2639_CR44","doi-asserted-by":"publisher","first-page":"2613","DOI":"10.1021\/bi00307a012","volume":"23","author":"TP Walsh","year":"1984","unstructured":"Walsh, T.P., Weber, A., Higgins, J., Bonder, E.M. & Mooseker, M.S. Effect of villin on the kinetics of actin polymerization. Biochemistry 23, 2613\u20132621 (1984).","journal-title":"Biochemistry"},{"key":"BFnsmb2639_CR45","doi-asserted-by":"publisher","first-page":"e00289","DOI":"10.1128\/mBio.00289-10","volume":"1","author":"VC Tam","year":"2010","unstructured":"Tam, V.C. et al. Functional analysis of VopF activity required for colonization in Vibrio cholerae. MBio. 1, e00289\u201310 (2010).","journal-title":"MBio."},{"key":"BFnsmb2639_CR46","doi-asserted-by":"publisher","first-page":"497","DOI":"10.1038\/nsmb.1792","volume":"17","author":"M Hernandez-Valladares","year":"2010","unstructured":"Hernandez-Valladares, M. et al. Structural characterization of a capping protein interaction motif defines a family of actin filament regulators. Nat. Struct. Mol. Biol. 17, 497\u2013503 (2010).","journal-title":"Nat. Struct. Mol. Biol."},{"key":"BFnsmb2639_CR47","doi-asserted-by":"publisher","first-page":"195","DOI":"10.1093\/bioinformatics\/bti770","volume":"22","author":"K Arnold","year":"2006","unstructured":"Arnold, K., Bordoli, L., Kopp, J. & Schwede, T. The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling. Bioinformatics 22, 195\u2013201 (2006).","journal-title":"Bioinformatics"},{"key":"BFnsmb2639_CR48","doi-asserted-by":"publisher","first-page":"2126","DOI":"10.1107\/S0907444904019158","volume":"60","author":"P Emsley","year":"2004","unstructured":"Emsley, P. & Cowtan, K. Coot: model-building tools for molecular graphics. Acta Crystallogr. D Biol. Crystallogr. 60, 2126\u20132132 (2004).","journal-title":"Acta Crystallogr. D Biol. Crystallogr."}],"container-title":["Nature Structural &amp; Molecular Biology"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/www.nature.com\/articles\/nsmb.2639.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/www.nature.com\/articles\/nsmb.2639","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/www.nature.com\/articles\/nsmb.2639.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,5,19]],"date-time":"2023-05-19T04:35:01Z","timestamp":1684470901000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.nature.com\/articles\/nsmb.2639"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2013,8,4]]},"references-count":48,"journal-issue":{"issue":"9","published-print":{"date-parts":[[2013,9]]}},"alternative-id":["BFnsmb2639"],"URL":"https:\/\/doi.org\/10.1038\/nsmb.2639","relation":{},"ISSN":["1545-9993","1545-9985"],"issn-type":[{"value":"1545-9993","type":"print"},{"value":"1545-9985","type":"electronic"}],"subject":[],"published":{"date-parts":[[2013,8,4]]}}}