Asymmetric Molecular Architecture of the Human γ-Tubulin Ring Complex

UCSF Chimera—A visualization system for exploratory research and analysis

Pettersen, E. F., Goddard, T. D., Huang, C. C., Couch, G. S., Greenblatt, D. M., Meng, E. C., & Ferrin, T. E. (2004) · Journal of Computational Chemistry · doi:10.1002/jcc.20084 · Cited by 45,260 · see citing works

Features and development of Coot

Emsley, P., Lohkamp, B., Scott, W. G., & Cowtan, K. D. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444910007493 · Cited by 27,510 · see citing works

MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification

Cox, J., & Mann, M. (2008) · Nature Biotechnology · doi:10.1038/nbt.1511 · Cited by 14,855 · see citing works

The Phyre2 web portal for protein modeling, prediction and analysis

Kelley, L. A., Mezulis, S., Yates, C. M., Wass, M. N., & Sternberg, M. J. E. (2015) · Nature Protocols · doi:10.1038/nprot.2015.053 · Cited by 9,652 · see citing works

MotionCor2 - anisotropic correction of beam-induced motion for improved cryo-electron microscopy

Zheng, S., Palovcak, E. J., Armache, J., Verba, K., Cheng, Y.-F., & Agard, D. (2017) · Nature Methods · doi:10.1038/nmeth.4193 · Cited by 7,678 · see citing works

Global quantification of mammalian gene expression control

Schwanhäusser, B., Busse, D., Li, N., Dittmar, G., Schuchhardt, J., Wolf, J., Chen, W., & Selbach, M. (2011) · Nature · doi:10.1038/nature10098 · Cited by 6,566 · see citing works

Automated electron microscope tomography using robust prediction of specimen movements.

Mastronarde, D. (2005) · Journal of Structural Biology · doi:10.1016/j.jsb.2005.07.007 · Cited by 5,446 · see citing works

CTFFIND4: Fast and accurate defocus estimation from electron micrographs

Rohou, A. L., & Grigorieff, N. (2015) · Journal of Structural Biology · doi:10.1016/j.jsb.2015.08.008 · Cited by 4,926 · see citing works

MolProbity: More and better reference data for improved all‐atom structure validation

Williams, C. J., Headd, J. J., Moriarty, N. W., Prisant, M. G., Videau, L. L., Deis, L. N., Verma, V., Keedy, D. A., Hintze, B. J., Chen, V. B., et al. (2018) · Protein Science · doi:10.1002/pro.3330 · Cited by 4,599 · see citing works

New tools for automated high-resolution cryo-EM structure determination in RELION-3

Zivanov, J., Nakane, T., Forsberg, B., Kimanius, D., Hagen, W., Lindahl, E., & Scheres, S. (2018) · eLife · doi:10.7554/elife.42166 · Cited by 4,377 · see citing works

Dynamic instability of microtubule growth

Mitchison, T., & Kirschner, M. (1984) · Nature · doi:10.1038/312237a0 · Cited by 3,337 · see citing works

EMAN2: An extensible image processing suite for electron microscopy

Tang, G., Peng, L., Baldwin, P. R., Mann, D. S., Jiang, W., Rees, I., & Ludtke, S. J. (2006) · Journal of Structural Biology · doi:10.1016/j.jsb.2006.05.009 · Cited by 2,914 · see citing works

Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy

Rosenthal, P. B., & Henderson, R. (2003) · Journal of Molecular Biology · doi:10.1016/j.jmb.2003.07.013 · Cited by 2,416 · see citing works

The Molecular Motor Toolbox for Intracellular Transport

Vale, R. D. (2003) · Cell · doi:10.1016/s0092-8674(03)00111-9 · Cited by 1,982 · see citing works

Quantifying the local resolution of cryo-EM density maps

Kucukelbir, A., Sigworth, F. J., & Tagare, H. D. (2013) · Nature Methods · doi:10.1038/nmeth.2727 · Cited by 1,847 · see citing works

JPred4: a protein secondary structure prediction server

Drozdetskiy, A., Cole, C., Procter, J. B., & Barton, G. J. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv332 · Cited by 1,714 · see citing works

Microtubule nucleation by γ-tubulin complexes

Kollman, J. M., Merdes, A., Mourey, L., & Agard, D. A. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3209 · Cited by 1,583 · see citing works

Beyond self-assembly: From microtubules to morphogenesis

Kirschner, M. W. (1986) · Cell · doi:10.1016/0092-8674(86)90318-1 · Cited by 1,362 · see citing works

Actin and Actin-Binding ProteinsPreprint

Pollard, T. D. (2016) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a018226 · Cited by 929 · see citing works

Nucleation of microtubule assembly by a γ-tubulin-containing ring complex

Zheng, Y., Wong, M. L., Alberts, B., & Mitchison, T. J. (1995) · Nature · doi:10.1038/378578a0 · Cited by 863 · see citing works

The quantitative proteome of a human cell line

Beck, M., Schmidt, A., Malmstroem, J., Claassen, M., Ori, A., Szymborska, A., Herzog, F., Rinner, O., Ellenberg, J., & Aebersold, R. (2011) · Molecular Systems Biology · doi:10.1038/msb.2011.82 · Cited by 816 · see citing works

The Centrosome Is a Selective Condensate that Nucleates Microtubules by Concentrating Tubulin

Woodruff, J. B., Gomes, B. F., Widlund, P. O., Mahamid, J., Honigmann, A., & Hyman, A. A. (2017) · Cell · doi:10.1016/j.cell.2017.05.028 · Cited by 685 · see citing works

Convergent Solutions to Binding at a Protein-Protein Interface

DeLano, W. L., Ultsch, M. H., de, A. M., Vos, & Wells, J. A. (2000) · Science · doi:10.1126/science.287.5456.1279 · Cited by 673 · see citing works

Identification of γ-tubulin, a new member of the tubulin superfamily encoded by mipA gene of Aspergillus nidulans

Oakley, C. E., & Oakley, B. R. (1989) · Nature · doi:10.1038/338662a0 · Cited by 627 · see citing works

Microtubule dynamics: an interplay of biochemistry and mechanics

Brouhard, G. J., & Rice, L. M. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0009-y · Cited by 569 · see citing works

Self-Organization of MTOCs Replaces Centrosome Function during Acentrosomal Spindle Assembly in Live Mouse Oocytes

Schuh, M., & Ellenberg, J. (2007) · Cell · doi:10.1016/j.cell.2007.06.025 · Cited by 568 · see citing works

γ-Tubulin is a highly conserved component of the centrosome

Stearns, T., Evans, L., & Kirschner, M. W. (1991) · Cell · doi:10.1016/0092-8674(91)90390-k · Cited by 564 · see citing works

Processing of Structurally Heterogeneous Cryo-EM Data in RELION

Scheres, S. H. W. (2016) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2016.04.012 · Cited by 550 · see citing works

Structure of the human 80S ribosome

Khatter, H., Myasnikov, A. G., Natchiar, S. K., & Klaholz, B. P. (2015) · Nature · doi:10.1038/nature14427 · Cited by 546 · see citing works

Systematic Analysis of Human Protein Complexes Identifies Chromosome Segregation Proteins

Hutchins, J. R. A., Toyoda, Y., Hegemann, B., Poser, I., Hèriché, J.-K., Sykora, M. M., Augsburg, M., Hudecz, O., Buschhorn, B. A., Bulkescher, J., et al. (2010) · Science · doi:10.1126/science.1181348 · Cited by 502 · see citing works

A robust pipeline for rapid production of versatile nanobody repertoires

Fridy, P. C., Li, Y., Keegan, S., Thompson, M. K., Nudelman, I., Scheid, J. F., Oeffinger, M., Nussenzweig, M. C., Fenyö, D., Chait, B. T., et al. (2014) · Nature Methods · doi:10.1038/nmeth.3170 · Cited by 493 · see citing works

In vitro reconstitution of centrosome assembly and function: The central role of γ-tubulin

Stearns, T., & Kirschner, M. W. (1994) · Cell · doi:10.1016/0092-8674(94)90503-7 · Cited by 456 · see citing works

The structure of the dynactin complex and its interaction with dynein

Urnavicius, L., Zhang, K., Diamant, A. G., Motz, C., Schlager, M. A., Yu, M., Patel, N. A., Robinson, C. V., & Carter, A. P. (2015) · Science · doi:10.1126/science.aaa4080 · Cited by 421 · see citing works

Augmin: a protein complex required for centrosome-independent microtubule generation within the spindle

Goshima, G., Mayer, M., Zhang, N., Stuurman, N., & Vale, R. D. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200711053 · Cited by 393 · see citing works

Branching Microtubule Nucleation in Xenopus Egg Extracts Mediated by Augmin and TPX2

Petry, S., Groen, A. C., Ishihara, K., Mitchison, T. J., & Vale, R. D. (2013) · Cell · doi:10.1016/j.cell.2012.12.044 · Cited by 376 · see citing works

MUSTER: Improving protein sequence profile–profile alignments by using multiple sources of structure information

Wu, S., & Zhang, Y. (2008) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.21945 · Cited by 375 · see citing works

Microtubule-dependent microtubule nucleation based on recruitment of γ-tubulin in higher plants

Murata, T., Sonobe, S., Baskin, T. I., Hyodo, S., Hasezawa, S., Nagata, T., Horio, T., & Hasebe, M. (2005) · Nature Cell Biology · doi:10.1038/ncb1306 · Cited by 360 · see citing works

Microtubule nucleation at the cis‐side of the Golgi apparatus requires AKAP450 and GM130

Rivero, S., Cardenas, J. M., Bornens, M., & Rios, R. M. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.47 · Cited by 319 · see citing works

GCP-WD is a γ-tubulin targeting factor required for centrosomal and chromatin-mediated microtubule nucleation

Lüders, J., Patel, U. K., & Stearns, T. (2005) · Nature Cell Biology · doi:10.1038/ncb1349 · Cited by 313 · see citing works

Characterization of Two Related Drosophila γ-tubulin Complexes that Differ in Their Ability to Nucleate Microtubules

Oegema, K., Wiese, C., Martin, O. C., Milligan, R. A., Iwamatsu, A., Mitchison, T. J., & Zheng, Y. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.144.4.721 · Cited by 308 · see citing works

Structure of the γ-tubulin ring complex: a template for microtubule nucleation

Moritz, M., Braunfeld, M. B., Guénebaut, V., Heuser, J., & Agard, D. A. (2000) · Nature Cell Biology · doi:10.1038/35014058 · Cited by 298 · see citing works

CDK5RAP2 Is a Pericentriolar Protein That Functions in Centrosomal Attachment of the γ-Tubulin Ring Complex

Fong, K.-W., Choi, Y.-K., Rattner, J. B., & Qi, R. Z. (2007) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-04-0371 · Cited by 283 · see citing works

Ultrastructural analysis of the dynactin complex: an actin-related protein is a component of a filament that resembles F-actin.

Schafer, D. A., Gill, S. R., Cooper, J. A., Heuser, J. E., & Schroer, T. A. (1994) · The Journal of Cell Biology · doi:10.1083/jcb.126.2.403 · Cited by 280 · see citing works

CDK5RAP2 stimulates microtubule nucleation by the γ-tubulin ring complex

Choi, Y.-K., Liu, P., Sze, S. K., Dai, C., & Qi, R. Z. (2010) · The Journal of Cell Biology · doi:10.1083/jcb.201007030 · Cited by 273 · see citing works

NEDD1-dependent recruitment of the γ-tubulin ring complex to the centrosome is necessary for centriole duplication and spindle assembly

Haren, L., Remy, M., Bazin, I., Callebaut, I., Wright, M., & Merdes, A. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200510028 · Cited by 261 · see citing works

The augmin complex plays a critical role in spindle microtubule generation for mitotic progression and cytokinesis in human cells

Uehara, R., Nozawa, R., Tomioka, A., Petry, S., Vale, R. D., Obuse, C., & Goshima, G. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0901587106 · Cited by 253 · see citing works

Preparation of Nuclear and Cytoplasmic Extracts from Mammalian Cells

Abmayr, S. M., Yao, T., Parmely, T. J., & Workman, J. L. (2006) · Current Protocols in Molecular Biology · doi:10.1002/0471142727.mb1201s75 · Cited by 252 · see citing works

Microtubule nucleating γ-TuSC assembles structures with 13-fold microtubule-like symmetry

Kollman, J. M., Polka, J., Zelter, A., Davis, T. N., & Agard, D. A. (2010) · Nature · doi:10.1038/nature09207 · Cited by 248 · see citing works

Molecular Architecture of SF3b and Structural Consequences of Its Cancer-Related Mutations

Cretu, C., Schmitzová, J., Ponce-Salvatierra, A., Dybkov, O., Laurentiis, E. I. D., Sharma, K., Will, C. L., Urlaub, H., Lührmann, R., & Peña, V. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.08.036 · Cited by 242 · see citing works

The architecture of the spliceosomal U4/U6.U5 tri-snRNP

Nguyen, T. H. D., Galej, W. P., Bai, X., Savva, C. G., Newman, A. J., Scheres, S. H. W., & Nagai, K. (2015) · Nature · doi:10.1038/nature14548 · Cited by 240 · see citing works

A new function for the γ -tubulin ring complex as a microtubule minus-end cap

Wiese, C., & Zheng, Y. (2000) · Nature Cell Biology · doi:10.1038/35014051 · Cited by 239 · see citing works

Current Protocols in Pharmacology

(2001) · John Wiley & Sons, Inc. eBooks · doi:10.1002/0471141755 · Cited by 237 · see citing works

The centrosome is an actin-organizing centre

Farina, F., Gaillard, J., Guérin, C., Couté, Y., Sillibourne, J., Blanchoin, L., & Théry, M. (2015) · Nature Cell Biology · doi:10.1038/ncb3285 · Cited by 235 · see citing works

The lattice as allosteric effector: Structural studies of αβ- and γ-tubulin clarify the role of GTP in microtubule assembly

Rice, L. M., Montabana, E. A., & Agard, D. A. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0801155105 · Cited by 229 · see citing works

Cep68 and Cep215 (Cdk5rap2) are required for centrosome cohesion

Graser, S., Stierhof, Y., & Nigg, E. A. (2007) · Journal of Cell Science · doi:10.1242/jcs.020248 · Cited by 218 · see citing works

Microtubule nucleation: beyond the template

Roostalu, J., & Surrey, T. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.75 · Cited by 197 · see citing works

Non-centrosomal nucleation mediated by augmin organizes microtubules in post-mitotic neurons and controls axonal microtubule polarity

Sánchez-Huertas, C., Freixo, F., Viais, R., Lacasa, C., Soriano, E., & Lüders, J. (2016) · Nature Communications · doi:10.1038/ncomms12187 · Cited by 195 · see citing works

Structural Basis of Interprotofilament Interaction and Lateral Deformation of Microtubules

Sui, H., & Downing, K. H. (2010) · Structure · doi:10.1016/j.str.2010.05.010 · Cited by 193 · see citing works

The spindle pole body component Spc97p interacts with the γ‐tubulin of Saccharomyces cerevisiae and functions in microtubule organization and spindle pole body duplication

Knop, M., Pereira, G., Geissler, S., Grein, K., & Schiebel, E. (1997) · The EMBO Journal · doi:10.1093/emboj/16.7.1550 · Cited by 188 · see citing works

GCP5 and GCP6: Two New Members of the Human γ-Tubulin Complex

Murphy, S. M., Preble, A. M., Patel, U. K., O'Connell, K. L., Dias, D. P., Moritz, M., Agard, D. A., Stults, J. T., & Stearns, T. (2001) · Molecular Biology of the Cell · doi:10.1091/mbc.12.11.3340 · Cited by 188 · see citing works

Insights into microtubule nucleation from the crystal structure of human γ-tubulin

Aldaz, H., Rice, L. M., Stearns, T., & Agard, D. A. (2005) · Nature · doi:10.1038/nature03586 · Cited by 185 · see citing works

A liquid-like spindle domain promotes acentrosomal spindle assembly in mammalian oocytes

So, C., Seres, K. B., Steyer, A. M., Mönnich, E. U., Clift, D., Pejkovska, A., Möbius, W., & Schuh, M. (2019) · Science · doi:10.1126/science.aat9557 · Cited by 167 · see citing works

Human β-Tubulin Isotypes Can Regulate Microtubule Protofilament Number and Stability

Ti, S.-C., Alushin, G. M., & Kapoor, T. M. (2018) · Developmental Cell · doi:10.1016/j.devcel.2018.08.014 · Cited by 158 · see citing works

Tubulin assembly sites and the organization of cytoplasmic microtubules in cultured mammalian cells.

Brinkley, B. R., Cox, S., Pepper, D. A., Wible, L., Brenner, S., & Pardue, R. L. (1981) · The Journal of Cell Biology · doi:10.1083/jcb.90.3.554 · Cited by 154 · see citing works

The mechanics of microtubule networks in cell division

Forth, S. T., & Kapoor, T. M. (2017) · The Journal of Cell Biology · doi:10.1083/jcb.201612064 · Cited by 153 · see citing works

The minus end in sight

Dammermann, A., Desai, A. B., & Oegema, K. (2003) · Current Biology · doi:10.1016/s0960-9822(03)00530-x · Cited by 144 · see citing works

Crystal Structures of Expressed Non-polymerizable Monomeric Actin in the ADP and ATP States

Rould, M. A., Wan, Q., Joel, P. B., Lowey, S., & Trybus, K. M. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m601973200 · Cited by 141 · see citing works

Microtubule nucleation by γ-tubulin complexes and beyond

Tovey, C. A., & Conduit, P. T. (2018) · Essays in Biochemistry · doi:10.1042/ebc20180028 · Cited by 139 · see citing works

Microtubule Nucleation Properties of Single Human γTuRCs Explained by Their Cryo-EM Structure

Consolati, T., Locke, J., Roostalu, J., Chen, Z. A., Gannon, J., Asthana, J., Lim, W. M., Martino, F., Cvetkovic, M. A., Rappsilber, J., et al. (2020) · Developmental Cell · doi:10.1016/j.devcel.2020.04.019 · Cited by 125 · see citing works

Ring closure activates yeast γTuRC for species-specific microtubule nucleation

Kollman, J. M., Greenberg, C. H., Li, S., Moritz, M., Zelter, A., Fong, K. K., Fernández, J., Šali, A., Kilmartin, J. V., Davis, T. N., et al. (2015) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2953 · Cited by 120 · see citing works

Immunostructural evidence for the template mechanism of microtubule nucleation

Keating, T. J., & Borisy, G. G. (2000) · Nature Cell Biology · doi:10.1038/35014045 · Cited by 117 · see citing works

Drosophila gamma-tubulin is part of a complex containing two previously identified centrosomal MAPs.

Raff, J. W., Kellogg, D. R., & Alberts, B. (1993) · The Journal of Cell Biology · doi:10.1083/jcb.121.4.823 · Cited by 114 · see citing works

Characterization and Reconstitution of Drosophila γ-Tubulin Ring Complex Subunits

Gunawardane, R. N., Martin, O. C., Cao, K., Zhang, L., Dej, K. J., Iwamatsu, A., & Zheng, Y. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.151.7.1513 · Cited by 112 · see citing works

The γTuRC Revisited: A Comparative Analysis of Interphase and Mitotic Human γTuRC Redefines the Set of Core Components and Identifies the Novel Subunit GCP8

Teixidó-Travesa, N., Villén, J., Lacasa, C., Bertran, M. T., Archinti, M., Gygi, S. P., Caelles, C., Roig, J., & Lüders, J. (2010) · Molecular Biology of the Cell · doi:10.1091/mbc.e10-05-0408 · Cited by 104 · see citing works

The Structure of the γ-Tubulin Small Complex: Implications of Its Architecture and Flexibility for Microtubule Nucleation

Kollman, J. M., Zelter, A., Muller, E. G., Fox, B., Rice, L. M., Davis, T. N., & Agard, D. A. (2007) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-09-0879 · Cited by 101 · see citing works

Purification of Tubulin from Porcine Brain

Gell, C., Friel, C. T., Borgonovo, B., Drechsel, D. N., Hyman, A. A., & Howard, J. (2011) · Methods in molecular biology · doi:10.1007/978-1-61779-252-6_2 · Cited by 89 · see citing works

Crystal structure of γ-tubulin complex protein GCP4 provides insight into microtubule nucleation

Guillet, V., Knibiehler, M., Gregory, L., Remy, M., Chemin, C., Raynaud‐Messina, B., Bon, C., Kollman, J. M., Agard, D. A., Merdes, A., et al. (2011) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2083 · Cited by 86 · see citing works

Comparison of the Native CCMV Virion within VitroAssembled CCMV Virions by Cryoelectron Microscopy and Image Reconstruction

Fox, J. M., Wang, G., Speir, J. A., Olson, N. H., Johnson, J. E., Baker, T. S., & Young, M. (1998) · Virology · doi:10.1006/viro.1998.9107 · Cited by 82 · see citing works

Divergent regulation of functionally distinct γ-tubulin complexes during differentiation

Muroyama, A., Seldin, L., & Lechler, T. (2016) · The Journal of Cell Biology · doi:10.1083/jcb.201601099 · Cited by 82 · see citing works

Reconstitution and Characterization of Budding Yeast γ-Tubulin Complex

Vinh, D. B. N., Kern, J. W., Hancock, W. O., Howard, J., & Davis, T. N. (2002) · Molecular Biology of the Cell · doi:10.1091/mbc.02-01-0607 · Cited by 76 · see citing works

Reconstitution of the augmin complex provides insights into its architecture and function

Hsia, K., Kubalek, E. W., Dottore, A., Hao, Q., Tsai, K., Forth, S. T., Shimamoto, Y., Milligan, R. A., & Kapoor, T. M. (2014) · Nature Cell Biology · doi:10.1038/ncb3030 · Cited by 73 · see citing works

NME7 is a functional component of the γ-tubulin ring complex

Liu, P., Choi, Y.-K., & Qi, R. Z. (2014) · Molecular Biology of the Cell · doi:10.1091/mbc.e13-06-0339 · Cited by 73 · see citing works

Vitrification after multiple rounds of sample application and blotting improves particle density on cryo-electron microscopy grids

Snijder, J., Borst, A. J., Dosey, A. M., Walls, A. C., Burrell, A. L., Reddy, V. S., Kollman, J. M., & Veesler, D. (2017) · Journal of Structural Biology · doi:10.1016/j.jsb.2017.02.008 · Cited by 73 · see citing works

MZT1 regulates microtubule nucleation by linking γTuRC assembly to adapter-mediated targeting and activation

Cota, R. R., Teixidó-Travesa, N., Ezquerra, A., Eibes, S., Lacasa, C., Roig, J., & Lüders, J. (2016) · Journal of Cell Science · doi:10.1242/jcs.195321 · Cited by 72 · see citing works

Coming into Focus: Mechanisms of Microtubule Minus-End Organization

Martin, M., & Akhmanova, A. S. (2018) · Trends in Cell Biology · doi:10.1016/j.tcb.2018.02.011 · Cited by 68 · see citing works

Soluble tubulin is significantly enriched at mitotic centrosomes

Baumgart, J., Kirchner, M., Redemann, S., Bond, A., Woodruff, J. B., Verbavatz, J., Jülicher, F., Müller‐Reichert, T., Hyman, A. A., & Jan Brugués, A. (2019) · The Journal of Cell Biology · doi:10.1083/jcb.201902069 · Cited by 44 · see citing works

Microtubule Cytoskeleton Remodeling by Acentriolar Microtubule-organizing Centers at the Entry and Exit from Mitosis inDrosophilaSomatic Cells

Moutinho-Pereira, S., Debec, A., & Maiato, H. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e09-01-0011 · Cited by 42 · see citing works

Functional Analysis of γ-Tubulin Complex Proteins Indicates Specific Lateral Association via Their N-terminal Domains

Farache, D., Jauneau, A., Chemin, C., Chartrain, M., Remy, M., Merdes, A., & Haren, L. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.744862 · Cited by 35 · see citing works

Preparation of Nuclear and Cytoplasmic Extracts from Mammalian Cells

Abmayr, S. M., Carrozza, M. J., & Workman, J. L. (2001) · Current Protocols in Pharmacology · doi:10.1002/0471141755.ph1203s12 · Cited by 26 · see citing works

Microtubules form by progressively faster tubulin accretion, not by nucleation–elongation

Rice, L. M., Moritz, M., & Agard, D. A. (2021) · The Journal of Cell Biology · doi:10.1083/jcb.202012079 · Cited by 16 · see citing works

The Atomic Structure of the Microtubule-Nucleating γ-Tubulin Small Complex and its Implications for RegulationPreprint

Brilot, A. F., & Agard, D. A. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/310813 · Cited by 2 · see citing works

Spc110 N-Terminal Domains Act Independently to Mediate Stable γ-Tubulin Small Complex Binding and γ-Tubulin Ring Complex AssemblyPreprint

Lyon, A. S., Zelter, A., Viswanath, S., Maxwell, A. M., Johnson, R. S., Yabut, K. C. B., MacCoss, M. J., Davis, T. N., Muller, E. G., Šali, A., et al. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/311027 · Cited by 2 · see citing works

Mechanisms of microtubule organization in differentiated animal cells

Akhmanova, A., & Kapitein, L. C. (2022) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-022-00473-y · Cited by 233 · see citing works

Microtubule Nucleation Properties of Single Human γTuRCs Explained by Their Cryo-EM Structure

Consolati, T., Locke, J., Roostalu, J., Chen, Z. A., Gannon, J., Asthana, J., Lim, W. M., Martino, F., Cvetkovic, M. A., Rappsilber, J., et al. (2020) · Developmental Cell · doi:10.1016/j.devcel.2020.04.019 · Cited by 125 · see citing works

Human centrosome organization and function in interphase and mitosis

Vásquez‐Limeta, A., & Lončarek, J. (2021) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2021.03.020 · Cited by 103 · see citing works

Polo-like kinase 1 independently controls microtubule-nucleating capacity and size of the centrosome

Ohta, M., Zhao, Z., Wu, D., Wang, S., Harrison, J. L., Gómez-Cavazos, J. S., Desai, A. B., & Oegema, K. (2020) · The Journal of Cell Biology · doi:10.1083/jcb.202009083 · Cited by 82 · see citing works

Mechanisms underlying spindle assembly and robustness

Valdez, V. A., Neahring, L., Petry, S., & Dumont, S. (2023) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-023-00584-0 · Cited by 75 · see citing works

Microtubule nucleation: The waltz between γ-tubulin ring complex and associated proteins

Liu, P., Würtz, M., Župa, E., Pfeffer, S., & Schiebel, E. (2020) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2020.10.004 · Cited by 73 · see citing works

Variable microtubule architecture in the malaria parasite

Ferreira, J. L., Pražák, V., Vasishtan, D., Siggel, M., Hentzschel, F., Binder, A. M., Pietsch, E., Kosinski, J., Frischknecht, F., Gilberger, T. W., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-36627-5 · Cited by 68 · see citing works

Cryo-EM and artificial intelligence visualize endogenous protein community members

Skalidis, I., Kyrilis, F. L., Tüting, C., Hamdi, F., Chojnowski, G., & Kastritis, P. L. (2022) · Structure · doi:10.1016/j.str.2022.01.001 · Cited by 61 · see citing works

The transition state and regulation of γ-TuRC-mediated microtubule nucleation revealed by single molecule microscopy

Thawani, A., Rale, M. J., Coudray, N., Bhabha, G., Stone, H. A., Shaevitz, J. W., & Petry, S. (2020) · eLife · doi:10.7554/elife.54253 · Cited by 61 · see citing works

Assembly of the asymmetric human γ-tubulin ring complex by RUVBL1-RUVBL2 AAA ATPase

Zimmermann, F., Serna, M., Ezquerra, A., Fernández-Leiro, R., Llorca, Ó., & Lüders, J. (2020) · Science Advances · doi:10.1126/sciadv.abe0894 · Cited by 60 · see citing works

MZT Proteins Form Multi-Faceted Structural Modules in the γ-Tubulin Ring Complex

Wieczorek, M., Huang, A. T.-L., Urnavicius, L., Hsia, K., & Kapoor, T. M. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.107791 · Cited by 56 · see citing works

Single-molecule sensing inside stereo- and regio-defined hetero-nanopores

Liu, W., Zhu, Q., Yang, C., Fu, Y., Zhang, J., Li, M., Yang, Z., Xin, K., Ma, J., Winterhalter, M., et al. (2024) · Nature Nanotechnology · doi:10.1038/s41565-024-01721-2 · Cited by 54 · see citing works

Centriole and PCM cooperatively recruit CEP192 to spindle poles to promote bipolar spindle assembly

Chinen, T., Yamazaki, K., Hashimoto, K., Fujii, K., Watanabe, K., Takeda, Y., Yamamoto, S., Nozaki, Y., Tsuchiya, Y., Takao, D., et al. (2020) · The Journal of Cell Biology · doi:10.1083/jcb.202006085 · Cited by 51 · see citing works

Sub-centrosomal mapping identifies augmin-γTuRC as part of a centriole-stabilizing scaffold

Schweizer, N., Haren, L., Dutto, I., Viais, R., Lacasa, C., Merdes, A., & Lüders, J. (2021) · Nature Communications · doi:10.1038/s41467-021-26252-5 · Cited by 50 · see citing works

Modular assembly of the principal microtubule nucleator γ-TuRC

Würtz, M., Župa, E., Atorino, E. S., Neuner, A., Böhler, A., Rahadian, A. S., Vermeulen, B. J. A., Tonon, G., Eustermann, S., Schiebel, E., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-28079-0 · Cited by 49 · see citing works

Shelterin is a dimeric complex with extensive structural heterogeneity

Zinder, J. C., Olinares, P. D. B., Svetlov, V., Bush, M. W., Nudler, E., Chait, B. T., Walz, T., & de Lange, T. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2201662119 · Cited by 44 · see citing works

Transition of human γ-tubulin ring complex into a closed conformation during microtubule nucleation

Brito, C., Serna, M., Guerra, P., Llorca, Ó., & Surrey, T. (2024) · Science · doi:10.1126/science.adk6160 · Cited by 46 · see citing works

Molecular insight into how γ-TuRC makes microtubules

Thawani, A., & Petry, S. (2021) · Journal of Cell Science · doi:10.1242/jcs.245464 · Cited by 43 · see citing works

Structure of the γ-tubulin ring complex-capped microtubule

Aher, A., Urnavicius, L., Xue, A., Neselu, K., & Kapoor, T. M. (2024) · Nature Structural & Molecular Biology · doi:10.1038/s41594-024-01264-z · Cited by 42 · see citing works

CAMSAP2 organizes a γ-tubulin-independent microtubule nucleation centre through phase separation

Imasaki, T., Kikkawa, S., Niwa, S., Saijo‐Hamano, Y., Shigematsu, H., Aoyama, K., Mitsuoka, K., Aoki, M., Sakamoto, A., Tomabechi, Y., et al. (2022) · eLife · doi:10.7554/elife.77365 · Cited by 40 · see citing works

CAMSAPs and nucleation-promoting factors control microtubule release from γ-TuRC

Rai, D., Song, Y., Hua, S., Stecker, K. E., Monster, J. L., Yin, V. C., Stucchi, R., Xu, Y., Zhang, Y., Chen, F., et al. (2024) · Nature Cell Biology · doi:10.1038/s41556-024-01366-2 · Cited by 38 · see citing works

Structure of the native γ-tubulin ring complex capping spindle microtubules

(2024) · doi:10.1038/s41594-024-01281-y · Cited by 38 · see citing works

The structure of the γ-TuRC: a 25-years-old molecular puzzle

Župa, E., Liu, P., Würtz, M., Schiebel, E., & Pfeffer, S. (2020) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2020.08.008 · Cited by 37 · see citing works

Biochemical reconstitutions reveal principles of human γ-TuRC assembly and function

Wieczorek, M., Ti, S.-C., Urnavicius, L., Molloy, K. R., Aher, A., Chait, B. T., & Kapoor, T. M. (2021) · The Journal of Cell Biology · doi:10.1083/jcb.202009146 · Cited by 36 · see citing works

CM1-driven assembly and activation of yeast γ-tubulin small complex underlies microtubule nucleation

Brilot, A. F., Lyon, A. S., Zelter, A., Viswanath, S., Maxwell, A. M., MacCoss, M. J., Muller, E. G., Šali, A., Davis, T. N., & Agard, D. A. (2021) · eLife · doi:10.7554/elife.65168 · Cited by 33 · see citing works

Budding of a Retrovirus: Some Assemblies Required

Rose, K. M., Hirsch, V. M., & Bouamr, F. (2020) · Viruses · doi:10.3390/v12101188 · Cited by 32 · see citing works

Micron-scale geometrical features of microtubules as regulators of microtubule organization

Mani, N., Wijeratne, S. S., & Subramanian, R. (2021) · eLife · doi:10.7554/elife.63880 · Cited by 34 · see citing works

Reconstitution and mechanistic dissection of the human microtubule branching machinery

Zhang, Y., Hong, X., Hua, S., & Jiang, K. (2022) · The Journal of Cell Biology · doi:10.1083/jcb.202109053 · Cited by 33 · see citing works

Autoinhibition of Cnn binding to γ-TuRCs prevents ectopic microtubule nucleation and cell division defects

Tovey, C. A., Tsuji, C., Egerton, A., Bernard, F., Guichet, A., de la Roche, M., & Conduit, P. T. (2021) · The Journal of Cell Biology · doi:10.1083/jcb.202010020 · Cited by 32 · see citing works

Microtubules Enhance Mesoscale Effective Diffusivity in the Crowded Metaphase Cytoplasm

Carlini, L., Brittingham, G. P., Holt, L. J., & Kapoor, T. M. (2020) · Developmental Cell · doi:10.1016/j.devcel.2020.07.020 · Cited by 31 · see citing works

γ-Tubulin in microtubule nucleation and beyond

Sulimenko, V., Dráberová, E., & Dráber, P. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.880761 · Cited by 31 · see citing works

Dysregulation of Microtubule Nucleating Proteins in Cancer Cells

Dráber, P., & Dráberová, E. (2021) · Cancers · doi:10.3390/cancers13225638 · Cited by 30 · see citing works

CDK5RAP2 activates microtubule nucleator γTuRC by facilitating template formation and actin release

Serna, M., Zimmermann, F., Vineethakumari, C., González-Rodríguez, N., Llorca, Ó., & Lüders, J. (2024) · Developmental Cell · doi:10.1016/j.devcel.2024.09.001 · Cited by 29 · see citing works

Small molecule-nanobody conjugate induced proximity controls intracellular processes and modulates endogenous unligandable targets

Sun, X., Zhou, C., Xia, S., & Chen, X. (2023) · Nature Communications · doi:10.1038/s41467-023-37237-x · Cited by 30 · see citing works

Molecular architecture of the augmin complex

Gabel, C. A., Li, Z., DeMarco, A. G., Zhang, Z., Yang, J., Hall, M. C., Barford, D., & Chang, L. (2022) · Nature Communications · doi:10.1038/s41467-022-33227-7 · Cited by 27 · see citing works

XMAP215 and γ-tubulin additively promote microtubule nucleation in purified solutions

King, B. R., Moritz, M., Kim, H., Agard, D. A., Asbury, C. L., & Davis, T. N. (2020) · Molecular Biology of the Cell · doi:10.1091/mbc.e20-02-0160 · Cited by 26 · see citing works

The augmin complex architecture reveals structural insights into microtubule branching

Župa, E., Würtz, M., Neuner, A., Hoffmann, T., Rettel, M., Böhler, A., Vermeulen, B. J. A., Eustermann, S., Schiebel, E., & Pfeffer, S. (2022) · Nature Communications · doi:10.1038/s41467-022-33228-6 · Cited by 26 · see citing works

Partial closure of the γ-tubulin ring complex by CDK5RAP2 activates microtubule nucleation

Xu, Y., Muñoz-Hernández, H., Krutyhołowa, R., Marxer, F., Cetin, F., & Wieczorek, M. (2024) · Developmental Cell · doi:10.1016/j.devcel.2024.09.002 · Cited by 32 · see citing works

The metaphase spindle at steady state – Mechanism and functions of microtubule poleward flux

Barišić, M., Rajendraprasad, G., & Steblyanko, Y. (2021) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2021.05.016 · Cited by 25 · see citing works

The conserved centrosomin motif, γTuNA, forms a dimer that directly activates microtubule nucleation by the γ-tubulin ring complex (γTuRC)

Rale, M. J., Romer, B., Mahon, B. P., Travis, S. M., & Petry, S. (2022) · eLife · doi:10.7554/elife.80053 · Cited by 25 · see citing works

Microtubule nucleation and γTuRC centrosome localization in interphase cells require ch-TOG

Ali, A., Vineethakumari, C., Lacasa, C., & Lüders, J. (2023) · Nature Communications · doi:10.1038/s41467-023-35955-w · Cited by 25 · see citing works

Molecular architectures of centrosomes in C. elegans embryos visualized by cryo-electron tomography

Tollervey, F., Rios, M. U., Zagoriy, I., Woodruff, J. B., & Mahamid, J. (2024) · Developmental Cell · doi:10.1016/j.devcel.2024.12.002 · Cited by 24 · see citing works

Distinct Microtubule Organizing Center Mechanisms Combine to Generate Neuron Polarity and Arbor Complexity

Wilkes, O. R., & Moore, A. W. (2020) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2020.594199 · Cited by 24 · see citing works

Microtubule Anchoring: Attaching Dynamic Polymers to Cellular Structures

Vineethakumari, C., & Lüders, J. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.867870 · Cited by 24 · see citing works

Microtubule‐associated proteins and enzymes modifying tubulin

Peng, N., & Nakamura, F. (2023) · Cytoskeleton · doi:10.1002/cm.21748 · Cited by 22 · see citing works

Microtubule nucleation for spindle assembly: one molecule at a time

Kraus, J., Alfaro‐Aco, R., Gouveia, B., & Petry, S. (2023) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2023.06.004 · Cited by 24 · see citing works

C53 Interacting with UFM1-Protein Ligase 1 Regulates Microtubule Nucleation in Response to ER Stress

Klebanovych, A., Vinopal, S., Dráberová, E., Sládková, V., Sulimenko, T., Sulimenko, V., Vosecká, V., Macůrek, L., Legido, A., & Dráber, P. (2022) · Cells · doi:10.3390/cells11030555 · Cited by 22 · see citing works

γ-TuRC asymmetry induces local protofilament mismatch at the RanGTP-stimulated microtubule minus end

Vermeulen, B. J. A., Böhler, A., Gao, Q., Neuner, A., Župa, E., Chu, Z., Würtz, M., Jäkle, U., Gruß, O. J., Pfeffer, S., et al. (2024) · The EMBO Journal · doi:10.1038/s44318-024-00087-4 · Cited by 21 · see citing works

A stable sub-complex between GCP4, GCP5 and GCP6 promotes the assembly of γ-tubulin ring complexes

Haren, L., Farache, D., Emorine, L. J., & Merdes, A. (2020) · Journal of Cell Science · doi:10.1242/jcs.244368 · Cited by 21 · see citing works

To nucleate or not, that is the question in neurons

Weiner, A. T., Thyagarajan, P., Shen, Y., & Rolls, M. M. (2021) · Neuroscience Letters · doi:10.1016/j.neulet.2021.135806 · Cited by 20 · see citing works

Profilin—A master coordinator of actin and microtubule organization in mammalian cells

Karlsson, R., & Dráber, P. (2021) · Journal of Cellular Physiology · doi:10.1002/jcp.30379 · Cited by 20 · see citing works

Potential Molecular Mechanisms of Rare Anti-Tumor Immune Response by SARS-CoV-2 in Isolated Cases of Lymphomas

Barh, D., Tiwari, S., Gomes, L. G. R., Weener, M. E., Alzahrani, K. J., Alsharif, K. F., Aljabali, A. A. A., Tambuwala, M. M., Lundstrom, K. H., Hassan, S. S., et al. (2021) · Viruses · doi:10.3390/v13101927 · Cited by 20 · see citing works

Microtubule-associated proteins promote microtubule generation in the absence of γ-tubulin in human colon cancer cells

Tsuchiya, K., & Goshima, G. (2021) · The Journal of Cell Biology · doi:10.1083/jcb.202104114 · Cited by 20 · see citing works

Structural mechanisms for centrosomal recruitment and organization of the microtubule nucleator γ-TuRC

Gao, Q., Hofer, F. W., Filbeck, S., Vermeulen, B. J. A., Würtz, M., Neuner, A., Kaplan, C., Žežlina, M., Sala, C., Shin, H., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-57729-2 · Cited by 22 · see citing works

How Microtubules Build the Spindle Branch by Branch

Travis, S. M., Mahon, B. P., & Petry, S. (2022) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-120420-114559 · Cited by 19 · see citing works

Understanding molecular mechanisms and predicting phenotypic effects of pathogenic tubulin mutations

Attard, T., Welburn, J. P. I., & Marsh, J. A. (2022) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1010611 · Cited by 18 · see citing works

Co-dependent formation of the Toxoplasma gondii subpellicular microtubules and inner membrane skeleton

Engelberg, K., Bauwens, C., Ferguson, D. J. P., & Gubbels, M. (2025) · mBio · doi:10.1128/mbio.01389-25 · Cited by 17 · see citing works

The gamma‐tubulin ring complex: Deciphering the molecular organization and assembly mechanism of a major vertebrate microtubule nucleator

Böhler, A., Vermeulen, B. J. A., Würtz, M., Župa, E., Pfeffer, S., & Schiebel, E. (2021) · BioEssays · doi:10.1002/bies.202100114 · Cited by 17 · see citing works

Autosomal recessive variants in TUBGCP2 alter the γ-tubulin ring complex leading to neurodevelopmental disease

Güngör, S., Oktay, Y., Hız, S., Aranguren‐Ibáñez, Á., Polat, İ., Yaramış, A., Karaca, E., Yiş, U., Sönmezler, E., Ekinci, B., et al. (2020) · iScience · doi:10.1016/j.isci.2020.101948 · Cited by 16 · see citing works

The actin regulator profilin 1 is functionally associated with the mammalian centrosome

Nejedlá, M., Klebanovych, A., Sulimenko, V., Sulimenko, T., Dráberová, E., Dráber, P., & Karlsson, R. (2020) · Life Science Alliance · doi:10.26508/lsa.202000655 · Cited by 16 · see citing works

Reconstitution of the recombinant human γ-tubulin ring complex

Würtz, M., Böhler, A., Neuner, A., Župa, E., Rohland, L., Liu, P., Vermeulen, B. J. A., Pfeffer, S., Eustermann, S., & Schiebel, E. (2021) · Open Biology · doi:10.1098/rsob.200325 · Cited by 16 · see citing works

Microtubules form by progressively faster tubulin accretion, not by nucleation–elongation

Rice, L. M., Moritz, M., & Agard, D. A. (2021) · The Journal of Cell Biology · doi:10.1083/jcb.202012079 · Cited by 16 · see citing works

The APC/C targets the Cep152–Cep63 complex at the centrosome to regulate mitotic spindle assembly

Tischer, T., Yang, J., & Barford, D. (2021) · Journal of Cell Science · doi:10.1242/jcs.259273 · Cited by 16 · see citing works

c-Abl kinase-mediated phosphorylation of γ-tubulin promotes γ-tubulin ring complexes assembly and microtubule nucleation

Wang, G., Dong, Q., Bai, Y., Gu, J., Tao, Q., Yue, J., Zhou, R., Niu, X., Zhu, L., Song, C., et al. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.101778 · Cited by 14 · see citing works

Autoinhibitory mechanism controls binding of centrosomin motif 1 to γ-tubulin ring complex

Yang, S., Au, F. K. C., Li, G., Lin, J., Li, X., & Qi, R. Z. (2023) · The Journal of Cell Biology · doi:10.1083/jcb.202007101 · Cited by 14 · see citing works

Multifaceted modes of γ-tubulin complex recruitment and microtubule nucleation at mitotic centrosomes

Zhu, Z., Bécam, I., Tovey, C. A., Elfarkouchi, A., Yen, E. C., Bernard, F., Guichet, A., & Conduit, P. T. (2023) · The Journal of Cell Biology · doi:10.1083/jcb.202212043 · Cited by 14 · see citing works

The fellowship of the RING: BRCA1, its partner BARD1 and their liaison in DNA repair and cancer

Russi, M., Marson, D., Fermeglia, A., Aulić, S., Fermeglia, M., Laurini, E., & Pricl, S. (2021) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2021.108009 · Cited by 13 · see citing works

Structural basis of protein condensation on microtubules underlying branching microtubule nucleation

Guo, C., Alfaro‐Aco, R., Zhang, C., Russell, R. W., Petry, S., & Polenova, T. E. (2023) · Nature Communications · doi:10.1038/s41467-023-39176-z · Cited by 14 · see citing works

Plant microtubule nucleating apparatus and its potential signaling pathway

Yagi, N., Fujita, S., & Nakamura, M. (2024) · Current Opinion in Plant Biology · doi:10.1016/j.pbi.2024.102624 · Cited by 12 · see citing works

Centrosomal and acentrosomal microtubule nucleation during neuronal development

Vinopal, S., & Bradke, F. (2025) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2025.103016 · Cited by 12 · see citing works

Lumenal components of cytoplasmic microtubules

Tsuji, C., & Dodding, M. P. (2022) · Biochemical Society Transactions · doi:10.1042/bst20220851 · Cited by 12 · see citing works

A nucleotide binding–independent role for γ-tubulin in microtubule capping and cell division

Berman, A. Y., Wieczorek, M., Aher, A., Olinares, P. D. B., Chait, B. T., & Kapoor, T. M. (2022) · The Journal of Cell Biology · doi:10.1083/jcb.202204102 · Cited by 13 · see citing works

Identification of Actin Filament-Associated Proteins in Giardia lamblia

Steele-Ogus, M. C., Johnson, R. S., MacCoss, M. J., & Paredez, A. R. (2021) · Microbiology Spectrum · doi:10.1128/spectrum.00558-21 · Cited by 11 · see citing works

PLK4 : Master Regulator of Centriole Duplication and Its Therapeutic Potential

Hamzah, M., Meitinger, F., & Ohta, M. (2025) · Cytoskeleton · doi:10.1002/cm.22031 · Cited by 10 · see citing works

Structure of the microtubule-anchoring factor NEDD1 bound to the γ-tubulin ring complex

Muñoz-Hernández, H., Xu, Y., Camardiel, A. P., Zhang, D. X., Xue, A., Aher, A., Walker, E., Marxer, F., Kapoor, T. M., & Wieczorek, M. (2025) · The Journal of Cell Biology · doi:10.1083/jcb.202410206 · Cited by 10 · see citing works

The cryo-EM structure of a γ-TuSC elucidates architecture and regulation of minimal microtubule nucleation systems

Župa, E., Zheng, A., Neuner, A., Würtz, M., Liu, P., Böhler, A., Schiebel, E., & Pfeffer, S. (2020) · Nature Communications · doi:10.1038/s41467-020-19456-8 · Cited by 10 · see citing works

Structure and assembly of the A-C linker connecting microtubule triplets in centrioles

Cai, B., Xu, J., Collet, E. H., Aarts, E., Luo, L., Leitner, A., Ishikawa, T., Beltrão, P., Pearson, C. G., Pilhofer, M., et al. (2025) · Science Advances · doi:10.1126/sciadv.ady3689 · Cited by 9 · see citing works

Moonlighting at the Poles: Non-Canonical Functions of Centrosomes

Langlois-Lemay, L., & D’Amours, D. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.930355 · Cited by 9 · see citing works

From tip to toe – dressing centrioles in γTuRC

Schweizer, N., & Lüders, J. (2021) · Journal of Cell Science · doi:10.1242/jcs.258397 · Cited by 9 · see citing works

The structure of the γ‐TuRC at the microtubule minus end – not just one solution

Gao, Q., Vermeulen, B. J. A., Würtz, M., Shin, H., Erdogdu, D., Zheng, A., Hofer, F. W., Neuner, A., Pfeffer, S., & Schiebel, E. (2024) · BioEssays · doi:10.1002/bies.202400117 · Cited by 8 · see citing works

Closure of the γ-tubulin ring complex by CDK5RAP2 activates microtubule nucleationPreprint

Xu, Y., Muñoz-Hernández, H., Krutyhołowa, R., Marxer, F., Cetin, F., & Wieczorek, M. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.12.14.571518 · Cited by 8 · see citing works

Microtubule choreography: spindle self-organization during cell division

Sridhara, A., & Shimamoto, Y. (2024) · Biophysical Reviews · doi:10.1007/s12551-024-01236-z · Cited by 7 · see citing works

γ-Tubulin Complexes and Fibrillar Arrays: Two Conserved High Molecular Forms with Many Cellular Functions

Chumová, J., Kourová, H., Trögelová, L., Daniel, G., & Binarová, P. (2021) · Cells · doi:10.3390/cells10040776 · Cited by 7 · see citing works

Disc and Actin Associated Protein 1 influences attachment in the intestinal parasite Giardia lamblia

Steele-Ogus, M. C., Obenaus, A. M., Sniadecki, N. J., & Paredez, A. R. (2022) · PLoS Pathogens · doi:10.1371/journal.ppat.1010433 · Cited by 7 · see citing works

Proteolysis of γ‐tubulin small complex proteins is mediated by the ubiquitin‐proteasome system

Yin, C., Lui, E. S. W., Jiang, T., & Qi, R. Z. (2021) · FEBS Letters · doi:10.1002/1873-3468.14146 · Cited by 6 · see citing works

Association of Hsp90 with p53 and Fizzy related homolog (Fzr) synchronizing Anaphase Promoting Complex (APC/C): An unexplored ally towards oncogenic pathway

Chowdhury, S. R., Koley, T., Singh, M., Ethayathulla, A. S., & Kaur, P. (2023) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2023.188883 · Cited by 6 · see citing works

TACC3–ch-TOG interaction regulates spindle microtubule assembly by controlling centrosomal recruitment of γ-TuRC

Rajeev, R., Mukhopadhyay, S., Bhagyanath, S., Priya, M. R. S. D., & Manna, T. K. (2023) · Bioscience Reports · doi:10.1042/bsr20221882 · Cited by 6 · see citing works

Native molecular architectures of centrosomes in C. elegans embryosPreprint

Tollervey, F., Rios, M. U., Zagoriy, I., Woodruff, J. B., & Mahamid, J. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.04.03.587742 · Cited by 6 · see citing works

Structural insights into the interplay between microtubule polymerases, γ-tubulin complexes and their receptors

Zheng, A., Vermeulen, B. J. A., Würtz, M., Neuner, A., Lübbehusen, N., Mayer, M. P., Schiebel, E., & Pfeffer, S. (2025) · Nature Communications · doi:10.1038/s41467-024-55778-7 · Cited by 5 · see citing works

Structural basis of human γTuRC closure during CM1-activated microtubule nucleation

Serna, M., Brito, C., Speroni, S., Zimmermann, F., López‐Perrote, A., Gili, M., Lacasa, C., Lüders, J., Surrey, T., & Llorca, Ó. (2026) · Nature Communications · doi:10.1038/s41467-026-70773-w · Cited by 5 · see citing works

A germline-specific role for unconventional components of the γ-tubulin complex in Caenorhabditis elegans

Haruta, N., Sumiyoshi, E., Honda, Y., Terasawa, M., Uchiyama, C., Toya, M., Kubota, Y., & Sugimoto, A. (2023) · Journal of Cell Science · doi:10.1242/jcs.260922 · Cited by 5 · see citing works

Conformational states of the microtubule nucleator, the γ-tubulin ring complexPreprint

Romer, B., Travis, S. M., Mahon, B. P., McManus, C. T., Jeffrey, P. D., Coudray, N., Raghu, R., Rale, M. J., Zhong, E. D., Bhabha, G., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.12.19.572162 · Cited by 5 · see citing works

NEDD1-S411 phosphorylation plays a critical function in the coordination of microtubule nucleation during mitosis

Timón, K., Scrofani, J., & Vernos, I. (2022) · Biology Open · doi:10.1242/bio.059474 · Cited by 4 · see citing works

Microtubule Nucleation by Single Human γTuRC in a Partly Open Asymmetric ConformationPreprint

Consolati, T., Locke, J., Roostalu, J., Asthana, J., Lim, W. M., Gannon, J., Martino, F., Costa, A., & Surrey, T. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/853218 · Cited by 4 · see citing works

CAMSAP-driven microtubule release from γ-TuRC and its regulation by nucleation-promoting factorsPreprint

Rai, D., Hua, S., Monster, J. L., Stucchi, R., Stecker, K. E., Zhang, Y., Katrukha, E. A., Altelaar, M. A. F., Wieczorek, M., Jiang, K., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.08.03.502613 · Cited by 4 · see citing works

Phosphorylation remodels the mitotic centrosome matrix to generate bipartite γ-tubulin complex docking sites

Ohta, M., Arakawa, O., Gu, Y., Tian, W., Corbett, K. D., Desai, A. B., & Oegema, K. (2026) · Science Advances · doi:10.1126/sciadv.aed6539 · Cited by 3 · see citing works

Cryo-EM structures of γ-TuRC reveal molecular insights into microtubule nucleation

Mammri, L., & Conduit, P. T. (2024) · Nature Structural & Molecular Biology · doi:10.1038/s41594-024-01345-z · Cited by 3 · see citing works

Centrosome: A Microtubule Nucleating Cellular Machinery

Jaiswal, S., Kasera, H., Jain, S. S., Khandelwal, S., & Singh, P. A. (2021) · Journal of the Indian Institute of Science · doi:10.1007/s41745-020-00213-1 · Cited by 3 · see citing works

The γ-TuRC: mastermind of multipurpose actions at the centrosome

Mukhopadhyay, S., Gao, Q., Manna, T. K., & Schiebel, E. (2026) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-026-06080-w · Cited by 2 · see citing works

Microtubule-Associated Proteins: From Dynamic Regulation of Microtubules to Cellular Architecture

Pais, E., & Schou, K. B. (2026) · Cells · doi:10.3390/cells15141289 · Cited by 2 · see citing works

Cryo-EM structures of the human reconstituted γ-tubulin complex

Li, S. (2022) · doi:10.14711/thesis-991013142358903412

Microtubule Nucleating Complexes: A structural view

Choy, R. M. (2013) · eScholarship (California Digital Library)

The structure of the γ‐TuRC at the microtubule minus end – not just one solution

Gao, Q., Vermeulen, B. J. A., Würtz, M., Shin, H., Erdogdu, D., Zheng, A., Hofer, F. W., Neuner, A., Pfeffer, S., & Schiebel, E. (2024) · BioEssays · doi:10.1002/bies.202400117 · Cited by 8 · see citing works

A stable sub-complex between GCP4, GCP5 and GCP6 promotes the assembly of γ-tubulin ring complexes

Haren, L., Farache, D., Emorine, L. J., & Merdes, A. (2020) · Journal of Cell Science · doi:10.1242/jcs.244368 · Cited by 21 · see citing works

Structural and functional mechanisms for centrosomal organization of γ-tubulin ring complex

Gao, Q. (2025) · heiDOK (Heidelberg University) · doi:10.11588/heidok.00037471