{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,27]],"date-time":"2026-09-27T06:10:52Z","timestamp":1790489452908,"version":"4.1.0"},"reference-count":42,"publisher":"National Academy of Sciences","issue":"20","license":[{"start":{"date-parts":[[2019,10,29]],"date-time":"2019-10-29T00:00:00Z","timestamp":1572307200000},"content-version":"vor","delay-in-days":183,"URL":"https:\/\/www.pnas.org\/site\/aboutpnas\/licenses.xhtml"}],"funder":[{"DOI":"10.13039\/501100001665","name":"Agence Nationale de la Recherche","doi-asserted-by":"publisher","award":["ANR-17-CE09-0040"],"award-info":[{"award-number":["ANR-17-CE09-0040"]}],"id":[{"id":"10.13039\/501100001665","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004097","name":"Fondation ARC pour la Recherche sur le Cancer","doi-asserted-by":"publisher","award":["PJA20161204544"],"award-info":[{"award-number":["PJA20161204544"]}],"id":[{"id":"10.13039\/501100004097","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001665","name":"Agence Nationale de la Recherche","doi-asserted-by":"publisher","award":["ANR-10-INSB-05-01"],"award-info":[{"award-number":["ANR-10-INSB-05-01"]}],"id":[{"id":"10.13039\/501100001665","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2019,5,14]]},"abstract":"<jats:p>\n                    Nucleation is one of the least understood steps of microtubule dynamics. It is a kinetically unfavorable process that is templated in the cell by the \u03b3-tubulin ring complex or by preexisting microtubules; it also occurs in vitro from pure tubulin. Here we study the nucleation inhibition potency of natural or artificial proteins in connection with their binding mode to the longitudinal surface of \u03b1- or \u03b2-tubulin. The structure of tubulin-bound CopN, a\n                    <jats:italic>Chlamydia<\/jats:italic>\n                    protein that delays nucleation, suggests that this protein may interfere with two protofilaments at the (+) end of a nucleus. Designed ankyrin repeat proteins that share a binding mode similar to that of CopN also impede nucleation, whereas those that target only one protofilament do not. In addition, an \u03b1Rep protein predicted to target two protofilaments at the (\u2212) end does not delay nucleation, pointing to different behaviors at both ends of the nucleus. Our results link the interference with protofilaments at the (+) end and the inhibition of nucleation.\n                  <\/jats:p>","DOI":"10.1073\/pnas.1813559116","type":"journal-article","created":{"date-parts":[[2019,4,29]],"date-time":"2019-04-29T22:51:11Z","timestamp":1556578271000},"page":"9859-9864","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":27,"title":["Insight into microtubule nucleation from tubulin-capping proteins"],"prefix":"10.1073","volume":"116","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-6407-6395","authenticated-orcid":false,"given":"Val\u00e9rie","family":"Campanacci","sequence":"first","affiliation":[{"name":"Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Universit\u00e9 Paris-Sud, Universit\u00e9 Paris-Saclay, 91198 Gif-sur-Yvette Cedex, France;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6077-859X","authenticated-orcid":false,"given":"Agathe","family":"Urvoas","sequence":"additional","affiliation":[{"name":"Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Universit\u00e9 Paris-Sud, Universit\u00e9 Paris-Saclay, 91198 Gif-sur-Yvette Cedex, France;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Soraya","family":"Cantos-Fernandes","sequence":"additional","affiliation":[{"name":"Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Universit\u00e9 Paris-Sud, Universit\u00e9 Paris-Saclay, 91198 Gif-sur-Yvette Cedex, France;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Magali","family":"Aumont-Nicaise","sequence":"additional","affiliation":[{"name":"Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Universit\u00e9 Paris-Sud, Universit\u00e9 Paris-Saclay, 91198 Gif-sur-Yvette Cedex, France;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ana-Andreea","family":"Arteni","sequence":"additional","affiliation":[{"name":"Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Universit\u00e9 Paris-Sud, Universit\u00e9 Paris-Saclay, 91198 Gif-sur-Yvette Cedex, France;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christophe","family":"Velours","sequence":"additional","affiliation":[{"name":"Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Universit\u00e9 Paris-Sud, Universit\u00e9 Paris-Saclay, 91198 Gif-sur-Yvette Cedex, France;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marie","family":"Valerio-Lepiniec","sequence":"additional","affiliation":[{"name":"Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Universit\u00e9 Paris-Sud, Universit\u00e9 Paris-Saclay, 91198 Gif-sur-Yvette Cedex, France;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Birgit","family":"Dreier","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, University of Zurich, CH-8057 Zurich, Switzerland;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4191-5306","authenticated-orcid":false,"given":"Andreas","family":"Pl\u00fcckthun","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, University of Zurich, CH-8057 Zurich, Switzerland;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Antoine","family":"Pilon","sequence":"additional","affiliation":[{"name":"INSERM UMR-S 1193, Universit\u00e9 Paris-Sud, Universit\u00e9 Paris-Saclay, 92296 Ch\u00e2tenay-Malabry, France;"},{"name":"Biochimie, APHP, H\u00f4pitaux Universitaires de l\u2019Est Parisien, 75571 Paris Cedex 12, France;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christian","family":"Po\u00fcs","sequence":"additional","affiliation":[{"name":"INSERM UMR-S 1193, Universit\u00e9 Paris-Sud, Universit\u00e9 Paris-Saclay, 92296 Ch\u00e2tenay-Malabry, France;"},{"name":"Biochimie-Hormonologie, APHP, H\u00f4pitaux Universitaires Paris-Sud, 92141 Clamart, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Philippe","family":"Minard","sequence":"additional","affiliation":[{"name":"Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Universit\u00e9 Paris-Sud, Universit\u00e9 Paris-Saclay, 91198 Gif-sur-Yvette Cedex, France;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5946-6759","authenticated-orcid":false,"given":"Beno\u00eet","family":"Gigant","sequence":"additional","affiliation":[{"name":"Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Universit\u00e9 Paris-Sud, Universit\u00e9 Paris-Saclay, 91198 Gif-sur-Yvette Cedex, France;"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[2019,4,29]]},"reference":[{"key":"e_1_3_4_1_2","doi-asserted-by":"crossref","first-page":"e19145","DOI":"10.7554\/eLife.19145","article-title":"Physical basis of large microtubule aster growth","volume":"5","author":"Ishihara K","year":"2016","unstructured":"Ishihara K, Korolev KS, Mitchison TJ (2016) Physical basis of large microtubule aster growth. eLife 5:e19145.","journal-title":"eLife"},{"key":"e_1_3_4_2_2","doi-asserted-by":"crossref","first-page":"768","DOI":"10.1016\/j.cell.2012.12.044","article-title":"Branching microtubule nucleation in Xenopus egg extracts mediated by augmin and TPX2","volume":"152","author":"Petry S","year":"2013","unstructured":"Petry S, Groen AC, Ishihara K, Mitchison TJ, Vale RD (2013) Branching microtubule nucleation in Xenopus egg extracts mediated by augmin and TPX2. Cell 152:768\u2013777.","journal-title":"Cell"},{"key":"e_1_3_4_3_2","doi-asserted-by":"crossref","first-page":"237","DOI":"10.1038\/312237a0","article-title":"Dynamic instability of microtubule growth","volume":"312","author":"Mitchison T","year":"1984","unstructured":"Mitchison T, Kirschner M (1984) Dynamic instability of microtubule growth. Nature 312:237\u2013242.","journal-title":"Nature"},{"key":"e_1_3_4_4_2","doi-asserted-by":"crossref","first-page":"1207","DOI":"10.1091\/mbc.E13-10-0594","article-title":"Dynamic instability 30 years later: Complexities in microtubule growth and catastrophe","volume":"26","author":"Brouhard GJ","year":"2015","unstructured":"Brouhard GJ (2015) Dynamic instability 30 years later: Complexities in microtubule growth and catastrophe. Mol Biol Cell 26:1207\u20131210.","journal-title":"Mol Biol Cell"},{"key":"e_1_3_4_5_2","doi-asserted-by":"crossref","first-page":"702","DOI":"10.1038\/nrm.2017.75","article-title":"Microtubule nucleation: Beyond the template","volume":"18","author":"Roostalu J","year":"2017","unstructured":"Roostalu J, Surrey T (2017) Microtubule nucleation: Beyond the template. Nat Rev Mol Cell Biol 18:702\u2013710.","journal-title":"Nat Rev Mol Cell Biol"},{"key":"e_1_3_4_6_2","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1016\/S0955-0674(02)00003-0","article-title":"Microtubule nucleation","volume":"15","author":"Job D","year":"2003","unstructured":"Job D, Valiron O, Oakley B (2003) Microtubule nucleation. Curr Opin Cell Biol 15:111\u2013117.","journal-title":"Curr Opin Cell Biol"},{"key":"e_1_3_4_7_2","doi-asserted-by":"crossref","first-page":"132","DOI":"10.1038\/nsmb.2953","article-title":"Ring closure activates yeast \u03b3TuRC for species-specific microtubule nucleation","volume":"22","author":"Kollman JM","year":"2015","unstructured":"Kollman JM, . (2015) Ring closure activates yeast \u03b3TuRC for species-specific microtubule nucleation. Nat Struct Mol Biol 22:132\u2013137.","journal-title":"Nat Struct Mol Biol"},{"key":"e_1_3_4_8_2","doi-asserted-by":"crossref","first-page":"575","DOI":"10.1038\/s41556-018-0091-6","article-title":"XMAP215 is a microtubule nucleation factor that functions synergistically with the \u03b3-tubulin ring complex","volume":"20","author":"Thawani A","year":"2018","unstructured":"Thawani A, Kadzik RS, Petry S (2018) XMAP215 is a microtubule nucleation factor that functions synergistically with the \u03b3-tubulin ring complex. Nat Cell Biol 20:575\u2013585.","journal-title":"Nat Cell Biol"},{"key":"e_1_3_4_9_2","doi-asserted-by":"crossref","first-page":"1681","DOI":"10.1016\/j.cub.2018.04.008","article-title":"The XMAP215 ortholog Alp14 promotes microtubule nucleation in fission yeast","volume":"28","author":"Flor-Parra I","year":"2018","unstructured":"Flor-Parra I, Iglesias-Romero AB, Chang F (2018) The XMAP215 ortholog Alp14 promotes microtubule nucleation in fission yeast. Curr Biol 28:1681\u20131691.e4.","journal-title":"Curr Biol"},{"key":"e_1_3_4_10_2","doi-asserted-by":"crossref","first-page":"1231","DOI":"10.1083\/jcb.116.5.1231","article-title":"The plus ends of stable microtubules are the exclusive nucleating structures for microtubules in the axon","volume":"116","author":"Baas PW","year":"1992","unstructured":"Baas PW, Ahmad FJ (1992) The plus ends of stable microtubules are the exclusive nucleating structures for microtubules in the axon. J Cell Biol 116:1231\u20131241.","journal-title":"J Cell Biol"},{"key":"e_1_3_4_11_2","doi-asserted-by":"crossref","first-page":"1422","DOI":"10.1038\/ncb3241","article-title":"Complementary activities of TPX2 and chTOG constitute an efficient importin-regulated microtubule nucleation module","volume":"17","author":"Roostalu J","year":"2015","unstructured":"Roostalu J, Cade NI, Surrey T (2015) Complementary activities of TPX2 and chTOG constitute an efficient importin-regulated microtubule nucleation module. Nat Cell Biol 17:1422\u20131434.","journal-title":"Nat Cell Biol"},{"key":"e_1_3_4_12_2","doi-asserted-by":"crossref","first-page":"907","DOI":"10.1038\/ncb3188","article-title":"Microtubule-associated proteins control the kinetics of microtubule nucleation","volume":"17","author":"Wieczorek M","year":"2015","unstructured":"Wieczorek M, Bechstedt S, Chaaban S, Brouhard GJ (2015) Microtubule-associated proteins control the kinetics of microtubule nucleation. Nat Cell Biol 17:907\u2013916.","journal-title":"Nat Cell Biol"},{"key":"e_1_3_4_13_2","doi-asserted-by":"crossref","first-page":"79","DOI":"10.1016\/S0092-8674(00)80961-7","article-title":"High-resolution model of the microtubule","volume":"96","author":"Nogales E","year":"1999","unstructured":"Nogales E, Whittaker M, Milligan RA, Downing KH (1999) High-resolution model of the microtubule. Cell 96:79\u201388.","journal-title":"Cell"},{"key":"e_1_3_4_14_2","doi-asserted-by":"crossref","first-page":"849","DOI":"10.1016\/j.cell.2015.07.012","article-title":"Mechanistic origin of microtubule dynamic instability and its modulation by EB proteins","volume":"162","author":"Zhang R","year":"2015","unstructured":"Zhang R, Alushin GM, Brown A, Nogales E (2015) Mechanistic origin of microtubule dynamic instability and its modulation by EB proteins. Cell 162:849\u2013859.","journal-title":"Cell"},{"key":"e_1_3_4_15_2","doi-asserted-by":"crossref","first-page":"607","DOI":"10.1038\/s41594-018-0087-8","article-title":"The role of tubulin-tubulin lattice contacts in the mechanism of microtubule dynamic instability","volume":"25","author":"Manka SW","year":"2018","unstructured":"Manka SW, Moores CA (2018) The role of tubulin-tubulin lattice contacts in the mechanism of microtubule dynamic instability. Nat Struct Mol Biol 25:607\u2013615.","journal-title":"Nat Struct Mol Biol"},{"key":"e_1_3_4_16_2","doi-asserted-by":"crossref","first-page":"7314","DOI":"10.1073\/pnas.1815823116","article-title":"Direct observation of individual tubulin dimers binding to growing microtubules","volume":"116","author":"Mickolajczyk KJ","year":"2019","unstructured":"Mickolajczyk KJ, Geyer EA, Kim T, Rice LM, Hancock WO (2019) Direct observation of individual tubulin dimers binding to growing microtubules. Proc Natl Acad Sci USA 116:7314\u20137322.","journal-title":"Proc Natl Acad Sci USA"},{"key":"e_1_3_4_17_2","doi-asserted-by":"crossref","first-page":"e3821","DOI":"10.1371\/journal.pone.0003821","article-title":"Tubulin dimers oligomerize before their incorporation into microtubules","volume":"3","author":"Mozziconacci J","year":"2008","unstructured":"Mozziconacci J, Sandblad L, Wachsmuth M, Brunner D, Karsenti E (2008) Tubulin dimers oligomerize before their incorporation into microtubules. PLoS One 3:e3821.","journal-title":"PLoS One"},{"key":"e_1_3_4_18_2","doi-asserted-by":"crossref","first-page":"391","DOI":"10.1038\/ncb3481","article-title":"Tubulin acetylation protects long-lived microtubules against mechanical ageing","volume":"19","author":"Portran D","year":"2017","unstructured":"Portran D, Schaedel L, Xu Z, Th\u00e9ry M, Nachury MV (2017) Tubulin acetylation protects long-lived microtubules against mechanical ageing. Nat Cell Biol 19:391\u2013398.","journal-title":"Nat Cell Biol"},{"key":"e_1_3_4_19_2","doi-asserted-by":"crossref","first-page":"112","DOI":"10.1038\/nature07355","article-title":"The essential role of the CopN protein in Chlamydia pneumoniae intracellular growth","volume":"456","author":"Huang J","year":"2008","unstructured":"Huang J, Lesser CF, Lory S (2008) The essential role of the CopN protein in Chlamydia pneumoniae intracellular growth. Nature 456:112\u2013115.","journal-title":"Nature"},{"key":"e_1_3_4_20_2","doi-asserted-by":"crossref","first-page":"33992","DOI":"10.1074\/jbc.M111.258426","article-title":"The Chlamydia effector chlamydial outer protein N (CopN) sequesters tubulin and prevents microtubule assembly","volume":"286","author":"Archuleta TL","year":"2011","unstructured":"Archuleta TL, . (2011) The Chlamydia effector chlamydial outer protein N (CopN) sequesters tubulin and prevents microtubule assembly. J Biol Chem 286:33992\u201333998.","journal-title":"J Biol Chem"},{"key":"e_1_3_4_21_2","doi-asserted-by":"crossref","first-page":"25199","DOI":"10.1074\/jbc.M114.568436","article-title":"Biochemical and structural insights into microtubule perturbation by CopN from Chlamydia pneumoniae","volume":"289","author":"Nawrotek A","year":"2014","unstructured":"Nawrotek A, . (2014) Biochemical and structural insights into microtubule perturbation by CopN from Chlamydia pneumoniae. J Biol Chem 289:25199\u201325210.","journal-title":"J Biol Chem"},{"key":"e_1_3_4_22_2","doi-asserted-by":"crossref","first-page":"489","DOI":"10.1146\/annurev-pharmtox-010611-134654","article-title":"Designed ankyrin repeat proteins (DARPins): Binding proteins for research, diagnostics, and therapy","volume":"55","author":"Pl\u00fcckthun A","year":"2015","unstructured":"Pl\u00fcckthun A (2015) Designed ankyrin repeat proteins (DARPins): Binding proteins for research, diagnostics, and therapy. Annu Rev Pharmacol Toxicol 55:489\u2013511.","journal-title":"Annu Rev Pharmacol Toxicol"},{"key":"e_1_3_4_23_2","doi-asserted-by":"crossref","first-page":"12011","DOI":"10.1073\/pnas.1204129109","article-title":"A designed ankyrin repeat protein selected to bind to tubulin caps the microtubule plus end","volume":"109","author":"Pecqueur L","year":"2012","unstructured":"Pecqueur L, . (2012) A designed ankyrin repeat protein selected to bind to tubulin caps the microtubule plus end. Proc Natl Acad Sci USA 109:12011\u201312016.","journal-title":"Proc Natl Acad Sci USA"},{"key":"e_1_3_4_24_2","doi-asserted-by":"crossref","first-page":"1155","DOI":"10.1091\/mbc.3.10.1155","article-title":"Role of GTP hydrolysis in microtubule dynamics: Information from a slowly hydrolyzable analogue, GMPCPP","volume":"3","author":"Hyman AA","year":"1992","unstructured":"Hyman AA, Salser S, Drechsel DN, Unwin N, Mitchison TJ (1992) Role of GTP hydrolysis in microtubule dynamics: Information from a slowly hydrolyzable analogue, GMPCPP. Mol Biol Cell 3:1155\u20131167.","journal-title":"Mol Biol Cell"},{"key":"e_1_3_4_25_2","doi-asserted-by":"crossref","first-page":"1350","DOI":"10.1016\/j.bbrc.2016.08.127","article-title":"Role of paclitaxel on critical nucleation concentration of tubulin and its effects thereof","volume":"478","author":"Verma S","year":"2016","unstructured":"Verma S, Kumar N, Verma V (2016) Role of paclitaxel on critical nucleation concentration of tubulin and its effects thereof. Biochem Biophys Res Commun 478:1350\u20131354.","journal-title":"Biochem Biophys Res Commun"},{"key":"e_1_3_4_26_2","doi-asserted-by":"crossref","first-page":"307","DOI":"10.1016\/j.jmb.2010.09.048","article-title":"Design, production and molecular structure of a new family of artificial alpha-helicoidal repeat proteins (\u03b1Rep) based on thermostable HEAT-like repeats","volume":"404","author":"Urvoas A","year":"2010","unstructured":"Urvoas A, . (2010) Design, production and molecular structure of a new family of artificial alpha-helicoidal repeat proteins (\u03b1Rep) based on thermostable HEAT-like repeats. J Mol Biol 404:307\u2013327.","journal-title":"J Mol Biol"},{"key":"e_1_3_4_27_2","doi-asserted-by":"crossref","first-page":"e71512","DOI":"10.1371\/journal.pone.0071512","article-title":"Selection of specific protein binders for pre-defined targets from an optimized library of artificial helicoidal repeat proteins (alphaRep)","volume":"8","author":"Guellouz A","year":"2013","unstructured":"Guellouz A, . (2013) Selection of specific protein binders for pre-defined targets from an optimized library of artificial helicoidal repeat proteins (alphaRep). PLoS One 8:e71512.","journal-title":"PLoS One"},{"key":"e_1_3_4_28_2","doi-asserted-by":"crossref","first-page":"497","DOI":"10.1016\/j.str.2018.12.001","article-title":"Selection and characterization of artificial proteins targeting the tubulin \u03b1 subunit","volume":"27","author":"Campanacci V","year":"2019","unstructured":"Campanacci V, . (2019) Selection and characterization of artificial proteins targeting the tubulin \u03b1 subunit. Structure 27:497\u2013506.e4.","journal-title":"Structure"},{"key":"e_1_3_4_29_2","doi-asserted-by":"crossref","unstructured":"Campanacci V Gigant B (2018) Tubulin-CopN-alphaRep complex. Protein Data bank. Available at https:\/\/www.rcsb.org\/structure\/6GX7. Deposited June 26 2018.","DOI":"10.2210\/pdb6gx7\/pdb"},{"key":"e_1_3_4_30_2","doi-asserted-by":"crossref","first-page":"28922","DOI":"10.1038\/srep28922","article-title":"Destabilizing an interacting motif strengthens the association of a designed ankyrin repeat protein with tubulin","volume":"6","author":"Ahmad S","year":"2016","unstructured":"Ahmad S, . (2016) Destabilizing an interacting motif strengthens the association of a designed ankyrin repeat protein with tubulin. Sci Rep 6:28922.","journal-title":"Sci Rep"},{"key":"e_1_3_4_31_2","unstructured":"Campanacci V Cantos-Fernandes S Gigant B (2018) Tubulin:TM-3 DARPin complex. Protein Data bank. Available at https:\/\/www.rcsb.org\/structure\/6GVN. Deposited June 21 2018."},{"key":"e_1_3_4_32_2","doi-asserted-by":"crossref","first-page":"e1004498","DOI":"10.1371\/journal.ppat.1004498","article-title":"A gatekeeper chaperone complex directs translocator secretion during type three secretion","volume":"10","author":"Archuleta TL","year":"2014","unstructured":"Archuleta TL, Spiller BW (2014) A gatekeeper chaperone complex directs translocator secretion during type three secretion. PLoS Pathog 10:e1004498.","journal-title":"PLoS Pathog"},{"key":"e_1_3_4_33_2","doi-asserted-by":"crossref","first-page":"418","DOI":"10.1016\/S0006-3495(97)78081-0","article-title":"Hydrolysis of GTP associated with the formation of tubulin oligomers is involved in microtubule nucleation","volume":"73","author":"Carlier MF","year":"1997","unstructured":"Carlier MF, Didry D, Pantaloni D (1997) Hydrolysis of GTP associated with the formation of tubulin oligomers is involved in microtubule nucleation. Biophys J 73:418\u2013427.","journal-title":"Biophys J"},{"key":"e_1_3_4_34_2","doi-asserted-by":"crossref","first-page":"5372","DOI":"10.1073\/pnas.74.12.5372","article-title":"Guanosinetriphosphatase activity of tubulin associated with microtubule assembly","volume":"74","author":"David-Pfeuty T","year":"1977","unstructured":"David-Pfeuty T, Erickson HP, Pantaloni D (1977) Guanosinetriphosphatase activity of tubulin associated with microtubule assembly. Proc Natl Acad Sci USA 74:5372\u20135376.","journal-title":"Proc Natl Acad Sci USA"},{"key":"e_1_3_4_35_2","doi-asserted-by":"crossref","first-page":"31085","DOI":"10.1074\/jbc.M112.383869","article-title":"Design and characterization of modular scaffolds for tubulin assembly","volume":"287","author":"Mignot I","year":"2012","unstructured":"Mignot I, . (2012) Design and characterization of modular scaffolds for tubulin assembly. J Biol Chem 287:31085\u201331094.","journal-title":"J Biol Chem"},{"key":"e_1_3_4_36_2","unstructured":"Campanacci V Cantos-Fernandes S Gigant B (2018) Tubulin:F3II DARPin complex. Protein Data bank. Available at https:\/\/www.rcsb.org\/structure\/6GVM. Deposited June 21 2018."},{"key":"e_1_3_4_37_2","doi-asserted-by":"crossref","first-page":"582","DOI":"10.1016\/j.cell.2011.06.053","article-title":"Rapid microtubule self-assembly kinetics","volume":"146","author":"Gardner MK","year":"2011","unstructured":"Gardner MK, . (2011) Rapid microtubule self-assembly kinetics. Cell 146:582\u2013592.","journal-title":"Cell"},{"key":"e_1_3_4_38_2","doi-asserted-by":"crossref","first-page":"711","DOI":"10.1038\/nrm4084","article-title":"Control of microtubule organization and dynamics: Two ends in the limelight","volume":"16","author":"Akhmanova A","year":"2015","unstructured":"Akhmanova A, Steinmetz MO (2015) Control of microtubule organization and dynamics: Two ends in the limelight. Nat Rev Mol Cell Biol 16:711\u2013726.","journal-title":"Nat Rev Mol Cell Biol"},{"key":"e_1_3_4_39_2","doi-asserted-by":"crossref","first-page":"3490","DOI":"10.1128\/JB.00203-11","article-title":"Scc1 (CP0432) and Scc4 (CP0033) function as a type III secretion chaperone for CopN of Chlamydia pneumoniae","volume":"193","author":"Silva-Herzog E","year":"2011","unstructured":"Silva-Herzog E, . (2011) Scc1 (CP0432) and Scc4 (CP0033) function as a type III secretion chaperone for CopN of Chlamydia pneumoniae. J Bacteriol 193:3490\u20133496.","journal-title":"J Bacteriol"},{"key":"e_1_3_4_40_2","doi-asserted-by":"crossref","first-page":"330","DOI":"10.1186\/s12866-014-0330-3","article-title":"Chlamydia pneumoniae effector chlamydial outer protein N sequesters fructose bisphosphate aldolase A, providing a benefit to bacterial growth","volume":"14","author":"Ishida K","year":"2014","unstructured":"Ishida K, Matsuo J, Yamamoto Y, Yamaguchi H (2014) Chlamydia pneumoniae effector chlamydial outer protein N sequesters fructose bisphosphate aldolase A, providing a benefit to bacterial growth. BMC Microbiol 14:330.","journal-title":"BMC Microbiol"},{"key":"e_1_3_4_41_2","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1007\/s00430-003-0206-x","article-title":"Expression and localization of type III secretion-related proteins of Chlamydia pneumoniae","volume":"193","author":"Lugert R","year":"2004","unstructured":"Lugert R, Kuhns M, Polch T, Gross U (2004) Expression and localization of type III secretion-related proteins of Chlamydia pneumoniae. Med Microbiol Immunol (Berl) 193:163\u2013171.","journal-title":"Med Microbiol Immunol (Berl)"},{"key":"e_1_3_4_42_2","doi-asserted-by":"crossref","first-page":"1066","DOI":"10.1016\/j.cell.2017.05.028","article-title":"The centrosome is a selective condensate that nucleates microtubules by concentrating tubulin","volume":"169","author":"Woodruff JB","year":"2017","unstructured":"Woodruff JB, . (2017) The centrosome is a selective condensate that nucleates microtubules by concentrating tubulin. Cell 169:1066\u20131077.e10.","journal-title":"Cell"}],"container-title":["Proceedings of the National Academy of Sciences"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/www.pnas.org\/syndication\/doi\/10.1073\/pnas.1813559116","content-type":"unspecified","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/pnas.org\/doi\/pdf\/10.1073\/pnas.1813559116","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,6,7]],"date-time":"2022-06-07T14:53:23Z","timestamp":1654613603000},"score":1,"resource":{"primary":{"URL":"https:\/\/pnas.org\/doi\/full\/10.1073\/pnas.1813559116"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2019,4,29]]},"references-count":42,"journal-issue":{"issue":"20","published-print":{"date-parts":[[2019,5,14]]}},"alternative-id":["10.1073\/pnas.1813559116"],"URL":"https:\/\/doi.org\/10.1073\/pnas.1813559116","relation":{},"ISSN":["0027-8424","1091-6490"],"issn-type":[{"value":"0027-8424","type":"print"},{"value":"1091-6490","type":"electronic"}],"subject":[],"published":{"date-parts":[[2019,4,29]]},"assertion":[{"value":"2019-04-29","order":2,"name":"published","label":"Published","group":{"name":"publication_history","label":"Publication History"}}]}}