{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T17:03:25Z","timestamp":1791306205319,"version":"4.3.1"},"reference-count":28,"publisher":"Springer Science and Business Media LLC","issue":"1","license":[{"start":{"date-parts":[[2004,12,12]],"date-time":"2004-12-12T00:00:00Z","timestamp":1102809600000},"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":[[2005,1]]},"DOI":"10.1038\/nsmb870","type":"journal-article","created":{"date-parts":[[2004,12,19]],"date-time":"2004-12-19T13:57:00Z","timestamp":1103464620000},"page":"26-31","source":"Crossref","is-referenced-by-count":169,"title":["Conformational changes in the Arp2\/3 complex leading to actin nucleation"],"prefix":"10.1038","volume":"12","author":[{"given":"Avital A","family":"Rodal","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Olga","family":"Sokolova","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Deborah B","family":"Robins","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Karen M","family":"Daugherty","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Simon","family":"Hippenmeyer","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Howard","family":"Riezman","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nikolaus","family":"Grigorieff","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bruce L","family":"Goode","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2004,12,12]]},"reference":[{"key":"BFnsmb870_CR1","doi-asserted-by":"publisher","first-page":"247","DOI":"10.1146\/annurev.cellbio.18.040202.112133","volume":"18","author":"MD Welch","year":"2002","unstructured":"Welch, M.D. & Mullins, R.D. Cellular control of actin nucleation. Annu. Rev. Cell Dev. Biol. 18, 247\u2013288 (2002).","journal-title":"Annu. Rev. Cell Dev. Biol."},{"key":"BFnsmb870_CR2","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":"BFnsmb870_CR3","doi-asserted-by":"publisher","first-page":"1903","DOI":"10.1016\/S0960-9822(01)00603-0","volume":"11","author":"J Zalevsky","year":"2001","unstructured":"Zalevsky, J., Lempert, L., Kranitz, H. & Mullins, R.D. Different WASP family proteins stimulate different Arp2\/3 complex-dependent actin-nucleating activities. Curr. Biol. 11, 1903\u20131913 (2001).","journal-title":"Curr. Biol."},{"key":"BFnsmb870_CR4","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":"BFnsmb870_CR5","doi-asserted-by":"publisher","first-page":"2456","DOI":"10.1126\/science.1063025","volume":"293","author":"N Volkmann","year":"2001","unstructured":"Volkmann, N. et al. Structure of Arp2\/3 complex in its activated state and in actin filament branch junctions. Science 293, 2456\u20132459 (2001).","journal-title":"Science"},{"key":"BFnsmb870_CR6","doi-asserted-by":"publisher","first-page":"1000","DOI":"10.1016\/S0960-9822(03)00383-X","volume":"13","author":"AA Rodal","year":"2003","unstructured":"Rodal, A.A., Manning, A.L., Goode, B.L. & Drubin, D.G. Negative regulation of yeast WASp by two SH3 domain-containing proteins. Curr. Biol. 13, 1000\u20131008 (2003).","journal-title":"Curr. Biol."},{"key":"BFnsmb870_CR7","doi-asserted-by":"publisher","first-page":"993","DOI":"10.1083\/jcb.200206113","volume":"159","author":"CL Humphries","year":"2002","unstructured":"Humphries, C.L. et al. Direct regulation of Arp2\/3 complex activity and function by the actin binding protein coronin. J. Cell Biol. 159, 993\u20131004 (2002).","journal-title":"J. Cell Biol."},{"key":"BFnsmb870_CR8","doi-asserted-by":"publisher","first-page":"331","DOI":"10.1083\/jcb.136.2.331","volume":"136","author":"RD Mullins","year":"1997","unstructured":"Mullins, R.D., Stafford, W.F. & Pollard, T.D. Structure, subunit topology, and actin-binding activity of the Arp2\/3 complex from Acanthamoeba . J. Cell Biol. 136, 331\u2013343 (1997).","journal-title":"J. Cell Biol."},{"key":"BFnsmb870_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":"BFnsmb870_CR10","doi-asserted-by":"publisher","first-page":"620","DOI":"10.1016\/S0960-9822(01)00152-X","volume":"11","author":"M Bailly","year":"2001","unstructured":"Bailly, M. et al. The F-actin side binding activity of the Arp2\/3 complex is essential for actin nucleation and lamellipod extension. Curr. Biol. 11, 620\u2013625 (2001).","journal-title":"Curr. Biol."},{"key":"BFnsmb870_CR11","doi-asserted-by":"publisher","first-page":"1041","DOI":"10.1016\/S1097-2765(01)00393-8","volume":"8","author":"H Gournier","year":"2001","unstructured":"Gournier, H., Goley, E.D., Niederstrasser, H., Trinh, T. & Welch, M.D. Reconstitution of human Arp2\/3 complex reveals critical roles of individual subunits in complex structure and activity. Mol. Cell 8, 1041\u20131052 (2001).","journal-title":"Mol. Cell"},{"key":"BFnsmb870_CR12","doi-asserted-by":"publisher","first-page":"385","DOI":"10.1038\/35017011","volume":"2","author":"D Pantaloni","year":"2000","unstructured":"Pantaloni, D., Boujemaa, R., Didry, D., Gounon, P. & Carlier, M.F. The Arp2\/3 complex branches filament barbed ends: functional antagonism with capping protein. Nat. Cell Biol. 2, 385\u2013391 (2000).","journal-title":"Nat. Cell Biol."},{"key":"BFnsmb870_CR13","doi-asserted-by":"crossref","first-page":"4533","DOI":"10.1242\/jcs.114.24.4533","volume":"114","author":"S Suetsugu","year":"2001","unstructured":"Suetsugu, S., Miki, H., Yamaguchi, H., Obinata, T., & Takenawa, T. Enhancement of branching efficiency by the actin filament-binding activity of N-WASP\/WAVE2. J. Cell Sci. 114, 4533\u20134542 (2001).","journal-title":"J. Cell Sci."},{"key":"BFnsmb870_CR14","doi-asserted-by":"publisher","first-page":"1319","DOI":"10.1083\/jcb.146.6.1319","volume":"146","author":"C Egile","year":"1999","unstructured":"Egile, C. et al. Activation of the CDC42 effector N-WASP by the Shigella flexneri IcsA protein promotes actin nucleation by Arp2\/3 complex and bacterial actin-based motility. J. Cell Biol. 146, 1319\u20131332 (1999).","journal-title":"J. Cell Biol."},{"key":"BFnsmb870_CR15","doi-asserted-by":"publisher","first-page":"14871","DOI":"10.1073\/pnas.261419298","volume":"98","author":"MJ Dayel","year":"2001","unstructured":"Dayel, M.J., Holleran, E.A. & Mullins, R.D. Arp2\/3 complex requires hydrolyzable ATP for nucleation of new actin filaments. Proc. Natl. Acad. Sci. USA 98, 14871\u201314876 (2001).","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"BFnsmb870_CR16","doi-asserted-by":"publisher","first-page":"46689","DOI":"10.1074\/jbc.C100476200","volume":"276","author":"C Le Clainche","year":"2001","unstructured":"Le Clainche, C., Didry, D., Carlier, M.F. & Pantaloni, D. Activation of Arp2\/3 complex by Wiskott-Aldrich syndrome protein is linked to enhanced binding of ATP to Arp2. J. Biol. Chem. 276, 46689\u201346692 (2001).","journal-title":"J. Biol. Chem."},{"key":"BFnsmb870_CR17","doi-asserted-by":"publisher","first-page":"6337","DOI":"10.1073\/pnas.1130513100","volume":"100","author":"C Le Clainche","year":"2003","unstructured":"Le Clainche, C., Pantaloni, D. & Carlier, M.F. ATP hydrolysis on actin-related protein 2\/3 complex causes debranching of dendritic actin arrays. Proc. Natl. Acad. Sci. USA 100, 6337\u20136342 (2003).","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"BFnsmb870_CR18","doi-asserted-by":"publisher","first-page":"E91","DOI":"10.1371\/journal.pbio.0020091","volume":"2","author":"MJ Dayel","year":"2004","unstructured":"Dayel, M.J. & Mullins, R.D. Activation of Arp2\/3 complex: addition of the first subunit of the new filament by a WASP protein triggers rapid ATP hydrolysis on Arp2. PLoS Biol. 2, E91 (2004).","journal-title":"PLoS Biol."},{"key":"BFnsmb870_CR19","doi-asserted-by":"publisher","first-page":"527","DOI":"10.1016\/0378-1119(88)90185-0","volume":"74","author":"RD Gietz","year":"1988","unstructured":"Gietz, R.D. & Sugino, A. New yeast\u2013Escherichia coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six\u2013base pair restriction sites. Gene 74, 527\u2013534 (1988).","journal-title":"Gene"},{"key":"BFnsmb870_CR20","doi-asserted-by":"publisher","first-page":"1311","DOI":"10.1083\/jcb.150.6.1311","volume":"150","author":"HN Higgs","year":"2000","unstructured":"Higgs, H.N. & Pollard, T.D. Activation by Cdc42 and PIP(2) of Wiskott-Aldrich syndrome protein (WASp) stimulates actin nucleation by Arp2\/3 complex. J. Cell Biol. 150, 1311\u20131320 (2000).","journal-title":"J. Cell Biol."},{"key":"BFnsmb870_CR21","doi-asserted-by":"publisher","first-page":"501","DOI":"10.1016\/S0960-9822(99)80218-8","volume":"9","author":"D Winter","year":"1999","unstructured":"Winter, D., Lechler, T. & Li, R. Activation of the yeast Arp2\/3 complex by Bee1p, a WASP-family protein. Curr. Biol. 9, 501\u2013504 (1999).","journal-title":"Curr. Biol."},{"key":"BFnsmb870_CR22","doi-asserted-by":"publisher","first-page":"17","DOI":"10.1006\/jsbi.1996.0004","volume":"116","author":"M Van Heel","year":"1996","unstructured":"Van Heel, M., Harauz, G., Orlova, E.V., Schmidt, R. & Schatz, M. A new generation of the IMAGIC image processing system. J. Struct. Biol. 116, 17\u201324 (1996).","journal-title":"J. Struct. Biol."},{"key":"BFnsmb870_CR23","first-page":"146","volume":"73","author":"G Harauz","year":"1986","unstructured":"Harauz, G. & van Heel, M. Exact filters for general geometry three-dimensional reconstruction. Optik 73, 146\u2013156 (1986).","journal-title":"Optik"},{"key":"BFnsmb870_CR24","doi-asserted-by":"publisher","first-page":"241","DOI":"10.1016\/0304-3991(92)90018-F","volume":"46","author":"J Frank","year":"1992","unstructured":"Frank, J. & Radermacher, M. Three-dimensional reconstruction of single particles negatively stained or in vitreous ice. Ultramicroscopy 46, 241\u2013262 (1992).","journal-title":"Ultramicroscopy"},{"key":"BFnsmb870_CR25","doi-asserted-by":"publisher","first-page":"190","DOI":"10.1006\/jsbi.1996.0030","volume":"116","author":"J Frank","year":"1996","unstructured":"Frank, J. et al. SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields. J. Struct. Biol. 116, 190\u2013199 (1996).","journal-title":"J. Struct. Biol."},{"key":"BFnsmb870_CR26","doi-asserted-by":"publisher","first-page":"1033","DOI":"10.1006\/jmbi.1998.1668","volume":"277","author":"N Grigorieff","year":"1998","unstructured":"Grigorieff, N. Three-dimensional structure of bovine NADH:ubiquinone oxidoreductase (complex I) at 22 \u00c5 in ice. J. Mol. Biol. 277, 1033\u20131046 (1998).","journal-title":"J. Mol. Biol."},{"key":"BFnsmb870_CR27","first-page":"724","volume":"1","author":"CC Huang","year":"1996","unstructured":"Huang, C.C., Couch, G.S., Pettersen, E.F. & Ferrin, T.E. Chimera: an extensible molecular modeling application constructed using standard components. Pac. Symp. Biocomput. 1, 724 (1996).","journal-title":"Pac. Symp. Biocomput."},{"key":"BFnsmb870_CR28","doi-asserted-by":"publisher","first-page":"185","DOI":"10.1006\/jsbi.1998.4080","volume":"125","author":"W Wriggers","year":"1999","unstructured":"Wriggers, W., Milligan, R. & McCammon, J. Situs: a package for docking crystal structures into low-resolution maps from electron microscopy. J. Struct. Biol. 125, 185\u2013195 (1999).","journal-title":"J. Struct. Biol."}],"container-title":["Nature Structural &amp; Molecular Biology"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/www.nature.com\/articles\/nsmb870.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/www.nature.com\/articles\/nsmb870","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/www.nature.com\/articles\/nsmb870.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,5,19]],"date-time":"2023-05-19T00:54:31Z","timestamp":1684457671000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.nature.com\/articles\/nsmb870"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2004,12,12]]},"references-count":28,"journal-issue":{"issue":"1","published-print":{"date-parts":[[2005,1]]}},"alternative-id":["BFnsmb870"],"URL":"https:\/\/doi.org\/10.1038\/nsmb870","relation":{},"ISSN":["1545-9993","1545-9985"],"issn-type":[{"value":"1545-9993","type":"print"},{"value":"1545-9985","type":"electronic"}],"subject":[],"published":{"date-parts":[[2004,12,12]]}}}