{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T20:13:25Z","timestamp":1791317605893,"version":"4.3.1"},"reference-count":54,"publisher":"Springer Science and Business Media LLC","issue":"1","license":[{"start":{"date-parts":[[2014,2,11]],"date-time":"2014-02-11T00:00:00Z","timestamp":1392076800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"},{"start":{"date-parts":[[2014,2,11]],"date-time":"2014-02-11T00:00:00Z","timestamp":1392076800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Nat Commun"],"DOI":"10.1038\/ncomms4308","type":"journal-article","created":{"date-parts":[[2014,2,11]],"date-time":"2014-02-11T14:13:46Z","timestamp":1392128026000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":72,"title":["Structural analysis of the transitional state of Arp2\/3 complex activation by two actin-bound WCAs"],"prefix":"10.1038","volume":"5","author":[{"given":"Malgorzata","family":"Boczkowska","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Grzegorz","family":"Rebowski","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"David J.","family":"Kast","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Roberto","family":"Dominguez","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2014,2,11]]},"reference":[{"key":"BFncomms4308_CR1","doi-asserted-by":"publisher","first-page":"453","DOI":"10.1016\/S0092-8674(03)00120-X","volume":"112","author":"TD Pollard","year":"2003","unstructured":"Pollard, T. D. & Borisy, G. G. Cellular motility driven by assembly and disassembly of actin filaments. Cell 112, 453\u2013465 (2003).","journal-title":"Cell"},{"key":"BFncomms4308_CR2","doi-asserted-by":"publisher","first-page":"404","DOI":"10.1038\/nrm1940","volume":"7","author":"M Kaksonen","year":"2006","unstructured":"Kaksonen, M., Toret, C. P. & Drubin, D. G. Harnessing actin dynamics for clathrin-mediated endocytosis. Nat. Rev. Mol. Cell. Biol. 7, 404\u2013414 (2006).","journal-title":"Nat. Rev. Mol. Cell. Biol."},{"key":"BFncomms4308_CR3","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-structure-function relationships. Crit. Rev. Biochem. Mol. Biol. 44, 351\u2013366 (2009).","journal-title":"Crit. Rev. Biochem. Mol. Biol."},{"key":"BFncomms4308_CR4","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":"BFncomms4308_CR5","doi-asserted-by":"publisher","first-page":"451","DOI":"10.1146\/annurev.biophys.35.040405.101936","volume":"36","author":"TD Pollard","year":"2007","unstructured":"Pollard, T. D. Regulation of actin filament assembly by Arp2\/3 complex and formins. Annu. Rev. Biophys. Biomol. Struct. 36, 451\u2013477 (2007).","journal-title":"Annu. Rev. Biophys. Biomol. Struct."},{"key":"BFncomms4308_CR6","doi-asserted-by":"publisher","first-page":"6181","DOI":"10.1073\/pnas.95.11.6181","volume":"95","author":"RD Mullins","year":"1998","unstructured":"Mullins, R. D., Heuser, J. A. & Pollard, T. D. The interaction of Arp2\/3 complex with actin: nucleation, high affinity pointed end capping, and formation of branching networks of filaments. Proc. Natl Acad. Sci. USA 95, 6181\u20136186 (1998).","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"BFncomms4308_CR7","doi-asserted-by":"publisher","first-page":"1679","DOI":"10.1126\/science.1066333","volume":"294","author":"RC Robinson","year":"2001","unstructured":"Robinson, R. C. et al. Crystal structure of Arp2\/3 complex. Science 294, 1679\u20131684 (2001).","journal-title":"Science"},{"key":"BFncomms4308_CR8","doi-asserted-by":"publisher","first-page":"887","DOI":"10.1083\/jcb.200709092","volume":"180","author":"I Rouiller","year":"2008","unstructured":"Rouiller, I. et al. The structural basis of actin filament branching by the Arp2\/3 complex. J. Cell Biol. 180, 887\u2013895 (2008).","journal-title":"J. Cell Biol."},{"key":"BFncomms4308_CR9","doi-asserted-by":"publisher","first-page":"3739","DOI":"10.1073\/pnas.96.7.3739","volume":"96","author":"LM Machesky","year":"1999","unstructured":"Machesky, L. M. et al. Scar, a WASp-related protein, activates nucleation of actin filaments by the Arp2\/3 complex. Proc. Natl Acad. Sci. USA 96, 3739\u20133744 (1999).","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"BFncomms4308_CR10","doi-asserted-by":"publisher","first-page":"1007","DOI":"10.1038\/35010008","volume":"404","author":"L Blanchoin","year":"2000","unstructured":"Blanchoin, L. et al. Direct observation of dendritic actin filament networks nucleated by Arp2\/3 complex and WASP\/Scar proteins. Nature 404, 1007\u20131011 (2000).","journal-title":"Nature"},{"key":"BFncomms4308_CR11","doi-asserted-by":"publisher","first-page":"269","DOI":"10.1016\/j.molcel.2004.09.018","volume":"16","author":"ED Goley","year":"2004","unstructured":"Goley, E. D., Rodenbusch, S. E., Martin, A. C. & Welch, M. D. Critical conformational changes in the Arp2\/3 complex are induced by nucleotide and nucleation promoting factor. Mol. Cell 16, 269\u2013279 (2004).","journal-title":"Mol. Cell"},{"key":"BFncomms4308_CR12","doi-asserted-by":"publisher","first-page":"15212","DOI":"10.1021\/bi991843+","volume":"38","author":"HN Higgs","year":"1999","unstructured":"Higgs, H. N., Blanchoin, L. & Pollard, T. D. Influence of the C terminus of Wiskott-Aldrich syndrome protein (WASp) and the Arp2\/3 complex on actin polymerization. Biochemistry 38, 15212\u201315222 (1999).","journal-title":"Biochemistry"},{"key":"BFncomms4308_CR13","doi-asserted-by":"publisher","first-page":"105","DOI":"10.1126\/science.281.5373.105","volume":"281","author":"MD Welch","year":"1998","unstructured":"Welch, M. D., Rosenblatt, J., Skoble, J., Portnoy, D. A. & Mitchison, T. J. Interaction of human Arp2\/3 complex and the Listeria monocytogenes ActA protein in actin filament nucleation. Science 281, 105\u2013108 (1998).","journal-title":"Science"},{"key":"BFncomms4308_CR14","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":"BFncomms4308_CR15","doi-asserted-by":"publisher","first-page":"591","DOI":"10.1038\/nsb952","volume":"10","author":"SC Panchal","year":"2003","unstructured":"Panchal, S. C., Kaiser, D. A., Torres, E., Pollard, T. D. & Rosen, M. K. A conserved amphipathic helix in WASP\/Scar proteins is essential for activation of Arp2\/3 complex. Nat. Struct. Biol. 10, 591\u2013598 (2003).","journal-title":"Nat. Struct. Biol."},{"key":"BFncomms4308_CR16","doi-asserted-by":"publisher","first-page":"217","DOI":"10.1016\/j.sbi.2009.12.012","volume":"20","author":"R Dominguez","year":"2010","unstructured":"Dominguez, R. Structural insights into de novo actin polymerization. Curr. Opin. Struct. Biol. 20, 217\u2013225 (2010).","journal-title":"Curr. Opin. Struct. Biol."},{"key":"BFncomms4308_CR17","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., Hanisch, 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":"BFncomms4308_CR18","doi-asserted-by":"publisher","first-page":"1285","DOI":"10.1073\/pnas.1211164110","volume":"110","author":"BA Smith","year":"2013","unstructured":"Smith, B. A., Daugherty-Clarke, K., Goode, B. L. & Gelles, J. Pathway of actin filament branch formation by Arp2\/3 complex revealed by single-molecule imaging. Proc. Natl Acad. Sci. USA 110, 1285\u20131290 (2013).","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"BFncomms4308_CR19","doi-asserted-by":"publisher","first-page":"10589","DOI":"10.1074\/jbc.M507470200","volume":"281","author":"AE Kelly","year":"2006","unstructured":"Kelly, A. E., Kranitz, H., Dotsch, V. & Mullins, R. D. Actin binding to the central domain of WASP\/Scar proteins plays a critical role in the activation of the Arp2\/3 complex. J. Biol. Chem. 281, 10589\u201310597 (2006).","journal-title":"J. Biol. Chem."},{"key":"BFncomms4308_CR20","doi-asserted-by":"publisher","first-page":"15247","DOI":"10.1021\/bi051065n","volume":"44","author":"M Kreishman-Deitrick","year":"2005","unstructured":"Kreishman-Deitrick, M. et al. NMR analyses of the activation of the Arp2\/3 complex by neuronal Wiskott-Aldrich syndrome protein. Biochemistry 44, 15247\u201315256 (2005).","journal-title":"Biochemistry"},{"key":"BFncomms4308_CR21","doi-asserted-by":"publisher","first-page":"1270","DOI":"10.1016\/S0960-9822(02)01035-7","volume":"12","author":"AM Weaver","year":"2002","unstructured":"Weaver, A. M. et al. Interaction of cortactin and N-WASp with Arp2\/3 complex. Curr. Biol. 12, 1270\u20131278 (2002).","journal-title":"Curr. Biol."},{"key":"BFncomms4308_CR22","doi-asserted-by":"publisher","first-page":"3468","DOI":"10.1074\/jbc.M006407200","volume":"276","author":"J Zalevsky","year":"2001","unstructured":"Zalevsky, J., Grigorova, I. & Mullins, R. D. Activation of the Arp2\/3 complex by the Listeria acta protein. Acta binds two actin monomers and three subunits of the Arp2\/3 complex. J. Biol. Chem. 276, 3468\u20133475 (2001).","journal-title":"J. Biol. Chem."},{"key":"BFncomms4308_CR23","doi-asserted-by":"publisher","first-page":"54629","DOI":"10.1074\/jbc.M402357200","volume":"279","author":"F Pan","year":"2004","unstructured":"Pan, F., Egile, C., Lipkin, T. & Li, R. ARPC1\/Arc40 mediates the interaction of the actin-related protein 2 and 3 complex with Wiskott-Aldrich syndrome protein family activators. J. Biol. Chem. 279, 54629\u201354636 (2004).","journal-title":"J. Biol. Chem."},{"key":"BFncomms4308_CR24","doi-asserted-by":"publisher","first-page":"695","DOI":"10.1016\/j.str.2008.02.013","volume":"16","author":"M Boczkowska","year":"2008","unstructured":"Boczkowska, M. et al. X-ray scattering study of activated Arp2\/3 complex with bound actin-WCA. Structure 16, 695\u2013704 (2008).","journal-title":"Structure"},{"key":"BFncomms4308_CR25","doi-asserted-by":"publisher","first-page":"E472","DOI":"10.1073\/pnas.1100236108","volume":"108","author":"SB Padrick","year":"2011","unstructured":"Padrick, S. B., Doolittle, L. K., Brautigam, C. A., King, D. S. & Rosen, M. K. Arp2\/3 complex is bound and activated by two WASP proteins. Proc. Natl Acad. Sci. USA 108, E472\u2013E479 (2011).","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"BFncomms4308_CR26","doi-asserted-by":"publisher","first-page":"E463","DOI":"10.1073\/pnas.1100125108","volume":"108","author":"SC Ti","year":"2011","unstructured":"Ti, S. C., Jurgenson, C. T., Nolen, B. J. & Pollard, T. D. Structural and biochemical characterization of two binding sites for nucleation-promoting factor WASp-VCA on Arp2\/3 complex. Proc. Natl Acad. Sci. USA 108, E463\u2013E471 (2011).","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"BFncomms4308_CR27","doi-asserted-by":"publisher","first-page":"426","DOI":"10.1016\/j.molcel.2008.10.012","volume":"32","author":"SB Padrick","year":"2008","unstructured":"Padrick, S. B. et al. Hierarchical regulation of WASP\/WAVE proteins. Mol. Cell 32, 426\u2013438 (2008).","journal-title":"Mol. Cell"},{"key":"BFncomms4308_CR28","doi-asserted-by":"publisher","first-page":"34646","DOI":"10.1074\/jbc.M112.394361","volume":"287","author":"JF Gaucher","year":"2012","unstructured":"Gaucher, J. F. et al. Interactions of isolated C-terminal fragments of neural Wiskott-Aldrich syndrome protein (N-WASP) with actin and Arp2\/3 complex. J. Biol. Chem. 287, 34646\u201334659 (2012).","journal-title":"J. Biol. Chem."},{"key":"BFncomms4308_CR29","doi-asserted-by":"publisher","first-page":"e4810","DOI":"10.1371\/journal.pone.0004810","volume":"4","author":"SA Koestler","year":"2009","unstructured":"Koestler, S. A. et al. F- and G-actin concentrations in lamellipodia of moving cells. PLoS One 4, e4810 (2009).","journal-title":"PLoS One"},{"key":"BFncomms4308_CR30","doi-asserted-by":"publisher","first-page":"76","DOI":"10.1038\/35050590","volume":"3","author":"JB Marchand","year":"2001","unstructured":"Marchand, J. B., Kaiser, D. A., Pollard, T. D. & Higgs, H. N. Interaction of WASP\/Scar proteins with actin and vertebrate Arp2\/3 complex. Nat. Cell Biol. 3, 76\u201382 (2001).","journal-title":"Nat. Cell Biol."},{"key":"BFncomms4308_CR31","doi-asserted-by":"publisher","first-page":"145","DOI":"10.1016\/j.str.2006.12.005","volume":"15","author":"SH Lee","year":"2007","unstructured":"Lee, S. H. et al. Structural basis for the actin-binding function of missing-in-metastasis. Structure 15, 145\u2013155 (2007).","journal-title":"Structure"},{"key":"BFncomms4308_CR32","doi-asserted-by":"publisher","first-page":"701","DOI":"10.1016\/j.chembiol.2013.03.019","volume":"20","author":"B Hetrick","year":"2013","unstructured":"Hetrick, B., Han, M. S., Helgeson, L. A. & Nolen, B. J. Small molecules CK-666 and CK-869 inhibit actin-related protein 2\/3 complex by blocking an activating conformational change. Chem. Biol. 20, 701\u2013712 (2013).","journal-title":"Chem. Biol."},{"key":"BFncomms4308_CR33","doi-asserted-by":"publisher","first-page":"376","DOI":"10.1038\/35014075","volume":"2","author":"WM Morton","year":"2000","unstructured":"Morton, W. M., Ayscough, K. R. & McLaughlin, P. J. Latrunculin alters the actin-monomer subunit interface to prevent polymerization. Nat. Cell Biol. 2, 376\u2013378 (2000).","journal-title":"Nat. Cell Biol."},{"key":"BFncomms4308_CR34","doi-asserted-by":"publisher","first-page":"11","DOI":"10.1016\/j.jmb.2010.08.040","volume":"403","author":"G Rebowski","year":"2010","unstructured":"Rebowski, G. et al. Structure of a longitudinal actin dimer assembled by tandem w domains: implications for actin filament nucleation. J. Mol. Biol. 403, 11\u201323 (2010).","journal-title":"J. Mol. Biol."},{"key":"BFncomms4308_CR35","doi-asserted-by":"publisher","first-page":"86","DOI":"10.1016\/S0014-5793(03)00934-7","volume":"552","author":"E Irobi","year":"2003","unstructured":"Irobi, E., Burtnick, L. D., Urosev, D., Narayan, K. & Robinson, R. C. From the first to the second domain of gelsolin: A common path on the surface of actin? FEBS Lett. 552, 86\u201390 (2003).","journal-title":"FEBS Lett."},{"key":"BFncomms4308_CR36","doi-asserted-by":"publisher","first-page":"826","DOI":"10.1038\/ncb1443","volume":"8","author":"AC Martin","year":"2006","unstructured":"Martin, A. C., Welch, M. D., Drubin, D. G. & Arp2\/3, A. T. P. hydrolysis-catalysed branch dissociation is critical for endocytic force generation. Nat. Cell Biol. 8, 826\u2013833 (2006).","journal-title":"Nat. Cell Biol."},{"key":"BFncomms4308_CR37","doi-asserted-by":"publisher","first-page":"4103","DOI":"10.1002\/j.1460-2075.1990.tb07632.x","volume":"9","author":"M Way","year":"1990","unstructured":"Way, M., Pope, B., Gooch, J., Hawkins, M. & Weeds, A. G. Identification of a region in segment 1 of gelsolin critical for actin binding. EMBO J. 9, 4103\u20134109 (1990).","journal-title":"EMBO J."},{"key":"BFncomms4308_CR38","doi-asserted-by":"publisher","first-page":"551","DOI":"10.1016\/j.jmb.2003.12.017","volume":"336","author":"CC Beltzner","year":"2004","unstructured":"Beltzner, C. C. & Pollard, T. D. Identification of functionally important residues of Arp2\/3 complex by analysis of homology models from diverse species. J. Mol. Biol. 336, 551\u2013565 (2004).","journal-title":"J. Mol. Biol."},{"key":"BFncomms4308_CR39","doi-asserted-by":"publisher","first-page":"861","DOI":"10.1016\/j.cub.2010.03.026","volume":"20","author":"M Gandhi","year":"2010","unstructured":"Gandhi, M. et al. GMF is a cofilin homolog that binds Arp2\/3 complex to stimulate filament debranching and inhibit actin nucleation. Curr. Biol. 20, 861\u2013867 (2010).","journal-title":"Curr. Biol."},{"key":"BFncomms4308_CR40","doi-asserted-by":"publisher","first-page":"25683","DOI":"10.1074\/jbc.C113.493338","volume":"288","author":"M Boczkowska","year":"2013","unstructured":"Boczkowska, M., Rebowski, G. & Dominguez, R. Glia maturation factor (GMF) interacts with Arp2\/3 complex in a nucleotide state-dependent manner. J. Biol. Chem. 288, 25683\u201325688 (2013).","journal-title":"J. Biol. Chem."},{"key":"BFncomms4308_CR41","doi-asserted-by":"publisher","first-page":"1062","DOI":"10.1038\/nsmb.2628","volume":"20","author":"Q Luan","year":"2013","unstructured":"Luan, Q. & Nolen, B. J. Structural basis for regulation of Arp2\/3 complex by GMF. Nat. Struct. Mol. Biol. 20, 1062\u20131068 (2013).","journal-title":"Nat. Struct. Mol. Biol."},{"key":"BFncomms4308_CR42","doi-asserted-by":"publisher","first-page":"14860","DOI":"10.1021\/bi991343g","volume":"38","author":"E Prochniewicz","year":"1999","unstructured":"Prochniewicz, E. & Thomas, D. D. Differences in structural dynamics of muscle and yeast actin accompany differences in functional interactions with myosin. Biochemistry 38, 14860\u201314867 (1999).","journal-title":"Biochemistry"},{"key":"BFncomms4308_CR43","doi-asserted-by":"publisher","first-page":"107","DOI":"10.1083\/jcb.127.1.107","volume":"127","author":"LM Machesky","year":"1994","unstructured":"Machesky, L. M., Atkinson, S. J., Ampe, C., Vandekerckhove, J. & Pollard, T. D. Purification of a cortical complex containing two unconventional actins from Acanthamoeba by affinity chromatography on profilin-agarose. J. Cell Biol. 127, 107\u2013115 (1994).","journal-title":"J. Cell Biol."},{"key":"BFncomms4308_CR44","doi-asserted-by":"publisher","first-page":"32531","DOI":"10.1074\/jbc.274.46.32531","volume":"274","author":"HN Higgs","year":"1999","unstructured":"Higgs, H. N. & Pollard, T. D. Regulation of actin polymerization by Arp2\/3 complex and WASp\/Scar proteins. J. Biol. Chem. 274, 32531\u201332534 (1999).","journal-title":"J. Biol. Chem."},{"key":"BFncomms4308_CR45","doi-asserted-by":"publisher","first-page":"449","DOI":"10.1016\/j.molcel.2007.04.017","volume":"26","author":"BJ Nolen","year":"2007","unstructured":"Nolen, B. J. & Pollard, T. D. Insights into the influence of nucleotides on actin family proteins from seven structures of Arp2\/3 complex. Mol. Cell 26, 449\u2013457 (2007).","journal-title":"Mol. Cell"},{"key":"BFncomms4308_CR46","doi-asserted-by":"publisher","first-page":"724","DOI":"10.1038\/nature09372","volume":"467","author":"T Fujii","year":"2010","unstructured":"Fujii, T., Iwane, A. H., Yanagida, T. & Namba, K. Direct visualization of secondary structures of F-actin by electron cryomicroscopy. Nature 467, 724\u2013728 (2010).","journal-title":"Nature"},{"key":"BFncomms4308_CR47","doi-asserted-by":"publisher","first-page":"151","DOI":"10.1038\/35004513","volume":"404","author":"AS Kim","year":"2000","unstructured":"Kim, A. S., Kakalis, L. T., Abdul-Manan, N., Liu, G. A. & Rosen, M. K. Autoinhibition and activation mechanisms of the Wiskott-Aldrich syndrome protein. Nature 404, 151\u2013158 (2000).","journal-title":"Nature"},{"key":"BFncomms4308_CR48","doi-asserted-by":"publisher","first-page":"169","DOI":"10.1146\/annurev-biophys-042910-155359","volume":"40","author":"R Dominguez","year":"2011","unstructured":"Dominguez, R. & Holmes, K. C. Actin structure and function. Annu. Rev. Biophys. 40, 169\u2013186 (2011).","journal-title":"Annu. Rev. Biophys."},{"key":"BFncomms4308_CR49","doi-asserted-by":"publisher","first-page":"572","DOI":"10.1016\/j.tibs.2004.09.004","volume":"29","author":"R Dominguez","year":"2004","unstructured":"Dominguez, R. Actin-binding proteins--a unifying hypothesis. Trends Biochem. Sci. 29, 572\u2013578 (2004).","journal-title":"Trends Biochem. Sci."},{"key":"BFncomms4308_CR50","doi-asserted-by":"publisher","first-page":"94","DOI":"10.1016\/j.ymeth.2011.07.005","volume":"55","author":"PD Adams","year":"2011","unstructured":"Adams, P. D. et al. The Phenix software for automated determination of macromolecular structures. Methods 55, 94\u2013106 (2011).","journal-title":"Methods"},{"key":"BFncomms4308_CR51","doi-asserted-by":"publisher","first-page":"236","DOI":"10.1038\/emboj.2011.343","volume":"31","author":"XP Xu","year":"2012","unstructured":"Xu, X. P. et al. Three-dimensional reconstructions of Arp2\/3 complex with bound nucleation promoting factors. EMBO J. 31, 236\u2013247 (2012).","journal-title":"EMBO J."},{"key":"BFncomms4308_CR52","doi-asserted-by":"publisher","first-page":"164","DOI":"10.1016\/0076-6879(82)85020-9","volume":"85","author":"JD Pardee","year":"1982","unstructured":"Pardee, J. D. & Spudich, J. A. Purification of muscle actin. Methods Enzymol. 85, (Pt B): 164\u2013181 (1982).","journal-title":"Methods Enzymol."},{"key":"BFncomms4308_CR53","doi-asserted-by":"publisher","first-page":"687","DOI":"10.1021\/ja00706a043","volume":"92","author":"TG Scott","year":"1970","unstructured":"Scott, T. G., Spencer, R. D., Leonard, N. J. & Weber, G. Emission properties of Nadh. Studies of fluorescence lifetimes and quantum efficiencies of Nadh, Acpyadh, and simplified synthetic models. J. Am. Chem. Soc. 92, 687 \u2013 (1970).","journal-title":"J. Am. Chem. Soc."},{"key":"BFncomms4308_CR54","doi-asserted-by":"publisher","first-page":"8207","DOI":"10.1073\/pnas.1001941107","volume":"107","author":"D Kast","year":"2010","unstructured":"Kast, D., Espinoza-Fonseca, L. M., Yi, C. & Thomas, D. D. Phosphorylation-induced structural changes in smooth muscle myosin regulatory light chain. Proc. Natl Acad. Sci. USA 107, 8207\u20138212 (2010).","journal-title":"Proc. Natl Acad. Sci. USA"}],"container-title":["Nature Communications"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.nature.com\/articles\/ncomms4308.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/ncomms4308","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/ncomms4308.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,1,6]],"date-time":"2023-01-06T03:56:43Z","timestamp":1672977403000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.nature.com\/articles\/ncomms4308"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2014,2,11]]},"references-count":54,"journal-issue":{"issue":"1","published-online":{"date-parts":[[2014,5,20]]}},"alternative-id":["BFncomms4308"],"URL":"https:\/\/doi.org\/10.1038\/ncomms4308","relation":{},"ISSN":["2041-1723"],"issn-type":[{"value":"2041-1723","type":"electronic"}],"subject":[],"published":{"date-parts":[[2014,2,11]]},"assertion":[{"value":"28 August 2013","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"22 January 2014","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"11 February 2014","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"The authors declare no competing financial interests.","order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Competing interests"}}],"article-number":"3308"}}