Structure of the DASH/Dam1 complex shows its role at the yeast kinetochore-microtubule interface

MUSCLE: multiple sequence alignment with high accuracy and high throughput

Edgar, R. C. (2004) · Nucleic Acids Research · doi:10.1093/nar/gkh340 · Cited by 44,662 · see citing works

<i>PHENIX</i> : a comprehensive Python-based system for macromolecular structure solution

Adams, P. D., Afonine, P. V., Bunkóczi, G., Chen, V. B., Davis, I. W., Echols, N., Headd, J. J., Hung, L.-W., Kapral, G. J., Grosse-Kunstleve, R. W., et al. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909052925 · Cited by 23,716 · see citing works

BLAST+: architecture and applications

Camacho, C., Coulouris, G., Avagyan, V., Ma, N., Papadopoulos, J., Bealer, K., & Madden, T. L. (2009) · BMC Bioinformatics · doi:10.1186/1471-2105-10-421 · Cited by 22,074 · see citing works

MAFFT: a novel method for rapid multiple sequence alignment based on fast Fourier transform

Katoh, K. (2002) · Nucleic Acids Research · doi:10.1093/nar/gkf436 · Cited by 17,027 · see citing works

<i>XDS</i>

Kabsch, W. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909047337 · Cited by 16,463 · see citing works

<i>MolProbity</i> : all-atom structure validation for macromolecular crystallography

Chen, V. B., Arendall, W. B., Headd, J. J., Keedy, D. A., Immormino, R. M., Kapral, G. J., Murray, L. W., Richardson, J. S., & Richardson, D. C. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909042073 · Cited by 14,115 · see citing works

Improved methods for building protein models in electron density maps and the location of errors in these models

Jones, T. A., Zou, J.-Y., Cowan, S. W., & Kjeldgaard, M. (1991) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767390010224 · Cited by 12,650 · see citing works

trimAl: a tool for automated alignment trimming in large-scale phylogenetic analyses

Capella-Gutiérrez, S., Silla-Martinez, J., & Gabaldón, T. (2009) · Bioinform. · doi:10.1093/bioinformatics/btp348 · Cited by 12,052 · see citing works

Enzymatic assembly of DNA molecules up to several hundred kilobases

Gibson, D. G., Young, L., Chuang, R.-Y., Venter, J. C., Hutchison, C. A., & Smith, H. O. (2009) · Nature Methods · doi:10.1038/nmeth.1318 · Cited by 9,742 · see citing works

EMBOSS: the European molecular biology open software suite.

Rice, P., Longden, I., & Bleasby, A. (2000) · Trends in Genetics · doi:10.1016/s0168-9525(00)02024-2 · Cited by 9,466 · 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

PHENIX: a comprehensive Python-based system for macromolecular structure solution

Adams, P. D., Afonine, P. V., Bunkòczi, G., Chen, V. B., Davis, I., Echols, N., Headd, J. J., Hung, L., Kapral, G. J., Grosse‐Kunstleve, R. W., et al. (2012) · International Tables for Crystallography · doi:10.1107/97809553602060000865 · Cited by 7,334 · see citing works

T-Coffee: A novel method for fast and accurate multiple sequence alignment.

Notredame, C., Higgins, D., & Heringa, J. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.4042 · Cited by 7,321 · see citing works

Deciphering key features in protein structures with the new ENDscript server

Robert, X., & Gouet, P. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku316 · Cited by 7,053 · see citing works

Biopython: freely available python tools for computational molecular biology and bioinformatics

Cock, P. J. A., Antao, T., Chang, J. T., Chapman, B. A., Cox, C. J., Dalke, A., Friedberg, I., Hamelryck, T., Kauff, F., Wilczynski, B., et al. (2009) · Bioinformatics · doi:10.1093/bioinformatics/btp163 · Cited by 6,080 · see citing works

Protein secondary structure prediction based on position-specific scoring matrices.

Jones, D. C. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.3091 · Cited by 5,741 · see citing works

RELION: Implementation of a Bayesian approach to cryo-EM structure determination

Scheres, S. H. W. (2012) · Journal of Structural Biology · doi:10.1016/j.jsb.2012.09.006 · 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

Global analysis of protein expression in yeast

Ghaemmaghami, S., Huh, W.-K., Bower, K., Howson, R. W., Belle, A., Dephoure, N., O'Shea, E. K., & Weissman, J. S. (2003) · Nature · doi:10.1038/nature02046 · Cited by 3,750 · see citing works

Gctf: Real-time CTF determination and correction

Zhang, K. (2015) · Journal of Structural Biology · doi:10.1016/j.jsb.2015.11.003 · Cited by 3,372 · see citing works

GenBank

Benson, D. A., Cavanaugh, M., Clark, K., Karsch-Mizrachi, I., Lipman, D. J., Ostell, J., & Sayers, E. W. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks1195 · Cited by 3,261 · see citing works

ConSurf 2016: An improved methodology to estimate and visualize evolutionary conservation in macromolecules

Ashkenazy, H., Abadi, S., Martz, E., Chay, O., Mayrose, I., Pupko, T., & Ben-Tal, N. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw408 · Cited by 3,163 · 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

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 1,763 · see citing works

MycoCosm portal: gearing up for 1000 fungal genomes

Grigoriev, I. V., Nikitin, R., Haridas, S., Kuo, A., Ohm, R., Otillar, R., Riley, R., Salamov, A., Zhao, X., Korzeniewski, F., et al. (2014) · Nucleic Acids Research · doi:10.1093/nar/gkt1183 · Cited by 1,498 · see citing works

Direct-coupling analysis of residue coevolution captures native contacts across many protein families

Morcos, F., Pagnani, A., Lunt, B., Bertolino, A., Marks, D. S., Sander, C., Zecchina, R., Onuchic, J. N., Hwa, T., & Weigt, M. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1111471108 · Cited by 1,434 · see citing works

AUGUSTUS: a web server for gene finding in eukaryotes

Stanke, M., Steinkamp, R., Waack, S., & Morgenstern, B. (2004) · Nucleic Acids Research · doi:10.1093/nar/gkh379 · Cited by 1,337 · see citing works

High-Resolution Comparative Modeling with RosettaCM

Song, Y., DiMaio, F., Wang, R. Y., Kim, D. E., Miles, C., Brunette, T., Thompson, J., & Baker, D. A. (2013) · Structure · doi:10.1016/j.str.2013.08.005 · Cited by 1,079 · see citing works

Measuring the optimal exposure for single particle cryo-EM using a 2.6 Å reconstruction of rotavirus VP6

Grant, T. S., & Grigorieff, N. (2015) · eLife · doi:10.7554/elife.06980 · Cited by 840 · see citing works

Automated tilt series alignment and tomographic reconstruction in IMOD

Mastronarde, D. N., & Held, S. R. (2016) · Journal of Structural Biology · doi:10.1016/j.jsb.2016.07.011 · Cited by 790 · see citing works

Tomato bushy stunt virus at 2.9 Å resolution

Harrison, S. C., Olson, A. J., Schutt, C. E., Winkler, F. K., & Bricogne, G. (1978) · Nature · doi:10.1038/276368a0 · Cited by 673 · see citing works

Improved contact prediction in proteins: using pseudolikelihoods to infer Potts models

Ekeberg, M., Lövkvist, C., Lan, Y., Weigt, M., & Aurell, E. (2013) · Physical Review E · doi:10.1103/physreve.87.012707 · Cited by 661 · see citing works

Phospho-Regulation of Kinetochore-Microtubule Attachments by the Aurora Kinase Ipl1p

Cheeseman, I. M., Anderson, S., Jwa, M., et al. (2002) · Cell · doi:10.1016/s0092-8674(02)00973-x · Cited by 616 · see citing works

PredictProtein—an open resource for online prediction of protein structural and functional features

Yachdav, G., Kloppmann, E., Kaján, L., Hecht, M., Goldberg, T., Hamp, T., Hönigschmid, P., Schafferhans, A., Roos, M., Bernhofer, M., et al. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku366 · Cited by 584 · see citing works

Three-Dimensional Structures of Membrane Proteins from Genomic Sequencing

Hopf, T. A., Colwell, L. J., Sheridan, R., Rost, B., Sander, C., & Marks, D. S. (2012) · Cell · doi:10.1016/j.cell.2012.04.012 · Cited by 501 · see citing works

SPIDER image processing for single-particle reconstruction of biological macromolecules from electron micrographs

Shaikh, T., Gao, H., Baxter, W., Asturias, F., Boisset, N., Leith, A., & Frank, J. (2008) · Nature Protocols · doi:10.1038/nprot.2008.156 · Cited by 499 · see citing works

Mechanistic Origin of Microtubule Dynamic Instability and Its Modulation by EB Proteins

Zhang, R., Alushin, G. M., Brown, A., & Nogales, E. (2015) · Cell · doi:10.1016/j.cell.2015.07.012 · Cited by 457 · see citing works

A robust algorithm for the reconstruction of helical filaments using single-particle methods

Egelman, E. H. (2000) · Ultramicroscopy · doi:10.1016/s0304-3991(00)00062-0 · Cited by 446 · see citing works

Three-dimensional ultrastructural analysis of the Saccharomyces cerevisiae mitotic spindle.

Winey, M., Mamay, C. L., O'Toole, E. T., Mastronarde, D. N., Giddings, T. H., McDonald, K. L., & McIntosh, J. R. (1995) · The Journal of Cell Biology · doi:10.1083/jcb.129.6.1601 · Cited by 434 · see citing works

Polewards chromosome movement driven by microtubule depolymerization in vitro

Koshland, D. E., Mitchison, T. J., & Kirschner, M. W. (1988) · Nature · doi:10.1038/331499a0 · Cited by 405 · see citing works

SPARX, a new environment for Cryo-EM image processing

Hohn, M. H., Tang, G., Goodyear, G., Baldwin, P. R., Huang, Z. X., Penczek, P. A., Yang, C., Glaeser, R. M., Adams, P. D., & Ludtke, S. J. (2006) · Journal of Structural Biology · doi:10.1016/j.jsb.2006.07.003 · Cited by 364 · see citing works

DelPhi: a comprehensive suite for DelPhi software and associated resources

Li, L., Li, C., Sarkar, S., Zhang, J., Witham, S., Zhang, Z., Wang, L., Smith, N., Petukh, M. G., & Alexov, E. G. (2012) · BMC Biophysics · doi:10.1186/2046-1682-5-9 · Cited by 336 · see citing works

The Ndc80 kinetochore complex forms oligomeric arrays along microtubules

Alushin, G. M., Ramey, V. H., Pasqualato, S., et al. (2010) · Nature · doi:10.1038/nature09423 · Cited by 305 · see citing works

Formation of a Dynamic Kinetochore- Microtubule Interface through Assembly of the Dam1 Ring Complex

Westermann, S., Avila-Sakar, A., Wang, H., et al. (2005) · Molecular Cell · doi:10.1016/j.molcel.2004.12.019 · Cited by 298 · see citing works

The yeast DASH complex forms closed rings on microtubules

Miranda, J. L., Wulf, P. D., Sorger, P. K., & Harrison, S. C. (2005) · Nature Structural & Molecular Biology · doi:10.1038/nsmb896 · Cited by 277 · see citing works

Centromere identity is specified by a single centromeric nucleosome in budding yeast

Furuyama, S., & Biggins, S. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0706985104 · Cited by 271 · see citing works

Molecular organization of the Ndc80 complex, an essential kinetochore component

Wei, R. R., Sorger, P. K., & Harrison, S. C. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0501168102 · Cited by 263 · see citing works

Structural Analysis of Multiprotein Complexes by Cross-linking, Mass Spectrometry, and Database Searching

Maiolica, A., Cittaro, D., Borsotti, D., Sennels, L., Ciferri, C., Tarricone, C., Musacchio, A., & Rappsilber, J. (2007) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m700274-mcp200 · Cited by 236 · see citing works

Cooperation of the Dam1 and Ndc80 kinetochore complexes enhances microtubule coupling and is regulated by aurora B

Tien, J. F., Umbreit, N. T., Gestaut, D. R., et al. (2010) · The Journal of Cell Biology · doi:10.1083/jcb.200910142 · Cited by 205 · see citing works

The Composition, Functions, and Regulation of the Budding Yeast Kinetochore

Biggins, S. (2013) · Genetics · doi:10.1534/genetics.112.145276 · Cited by 197 · see citing works

SCaFoS: a tool for Selection, Concatenation and Fusion of Sequences for phylogenomics

Roure, B., Rodríguez‐Ezpeleta, N., & Philippe, H. (2007) · BMC Evolutionary Biology · doi:10.1186/1471-2148-7-s1-s2 · Cited by 190 · see citing works

Fast pseudolikelihood maximization for direct-coupling analysis of protein structure from many homologous amino-acid sequences

Ekeberg, M., Hartonen, T., & Aurell, E. M. (2014) · Journal of Computational Physics · doi:10.1016/j.jcp.2014.07.024 · Cited by 184 · see citing works

Architecture of the Human Ndc80-Hec1 Complex, a Critical Constituent of the Outer Kinetochore

Ciferri, C., Luca, J. D., Monzani, S., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m504070200 · Cited by 182 · see citing works

Frealign

Grigorieff, N. (2016) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2016.04.013 · Cited by 181 · see citing works

De novo protein structure determination from near-atomic-resolution cryo-EM maps

Wang, R. Y., Kudryashev, M., Li, X., Egelman, E. H., Basler, M., Cheng, Y., Baker, D. A., & DiMaio, F. (2015) · Nature Methods · doi:10.1038/nmeth.3287 · Cited by 180 · see citing works

Diffraction-geometry refinement in theDIALSframework

Waterman, D. G., Winter, G., Gildea, R. J., et al. (2016) · Acta Crystallographica Section D Structural Biology · doi:10.1107/s2059798316002187 · Cited by 175 · see citing works

The Dam1 complex confers microtubule plus end–tracking activity to the Ndc80 kinetochore complex

Lampert, F., Hornung, P., & Westermann, S. (2010) · The Journal of Cell Biology · doi:10.1083/jcb.200912021 · Cited by 168 · see citing works

Molecular mechanisms of microtubule-dependent kinetochore transport toward spindle poles

Tanaka, K., Kitamura, E., Kitamura, Y., & Tanaka, T. U. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200702141 · Cited by 164 · see citing works

Structural and Functional Organization of the Ska Complex, a Key Component of the Kinetochore-Microtubule Interface

Jeyaprakash, A. A., Santamaría, A., Jayachandran, U., et al. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.03.005 · Cited by 161 · see citing works

High resolution single particle refinement in EMAN2.1

Bell, J. M., Chen, M., Baldwin, P. R., & Ludtke, S. J. (2016) · Methods · doi:10.1016/j.ymeth.2016.02.018 · Cited by 155 · see citing works

Phosphoregulation and depolymerization-driven movement of the Dam1 complex do not require ring formation

Gestaut, D. R., Graczyk, B., Cooper, J. R., et al. (2008) · Nature Cell Biology · doi:10.1038/ncb1702 · Cited by 142 · see citing works

Molecular basis of outer kinetochore assembly on CENP-T

Veld, P. J. H. I. ’., Jeganathan�, S., Petrović, A., et al. (2016) · eLife · doi:10.7554/elife.21007 · Cited by 127 · see citing works

Structure of the MIND Complex Defines a Regulatory Focus for Yeast Kinetochore Assembly

Dimitrova, Y. N., Jenni, S., Valverde, R., Khin, Y., & Harrison, S. C. (2016) · Cell · doi:10.1016/j.cell.2016.10.011 · Cited by 121 · see citing works

Microtubule depolymerization can drive poleward chromosome motion in fission yeast

Grishchuk, E. L., & McIntosh, J. R. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601353 · Cited by 118 · see citing works

Plasticity in protein–DNA recognition: lac repressor interacts with its natural operator O1 through alternative conformations of its DNA‐binding domain

Kalodimos, C. G., Bonvin, A. M. J. J., Salinas, R. K., Wechselberger, R. W., Boelens, R., & Kaptein, R. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf318 · Cited by 118 · see citing works

Analysis of kinesin motor function at budding yeast kinetochores

Tytell, J. D., & Sorger, P. K. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200509101 · Cited by 116 · see citing works

Automatic estimation and correction of anisotropic magnification distortion in electron microscopes

Grant, T. S., & Grigorieff, N. (2015) · Journal of Structural Biology · doi:10.1016/j.jsb.2015.08.006 · Cited by 110 · see citing works

Architecture and Flexibility of the Yeast Ndc80 Kinetochore Complex

Wang, H., Long, S., Ciferri, C., Westermann, S., Drubin, D. G., Barnes, G., & Nogales, E. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.08.077 · Cited by 110 · see citing works

The protelomerase of temperate Escherichia coli phage N15 has cleaving-joining activity

Deneke, J., Ziegelin, G., Lurz, R., & Lanka, E. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.14.7721 · Cited by 103 · see citing works

SPRING – An image processing package for single-particle based helical reconstruction from electron cryomicrographs

Desfosses, A., Ciuffa, R., Gutsche, I., et al. (2013) · Journal of Structural Biology · doi:10.1016/j.jsb.2013.11.003 · Cited by 100 · see citing works

The Ndc80 Loop Region Facilitates Formation of Kinetochore Attachment to the Dynamic Microtubule Plus End

Maure, J.-F., Komoto, S., Oku, Y., et al. (2011) · Current Biology · doi:10.1016/j.cub.2010.12.050 · Cited by 96 · see citing works

Architecture of the Dam1 kinetochore ring complex and implications for microtubule-driven assembly and force-coupling mechanisms

Wang, H., Ramey, V. H., Westermann, S., Leschziner, A. E., Welburn, J. P. I., Nakajima, Y., Drubin, D. G., Barnes, G., & Nogales, E. (2007) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1274 · Cited by 91 · see citing works

Structural Analysis of Lac Repressor Bound to Allosteric Effectors

Daber, R. D., Stayrook, S. E., Rosenberg, A. F., et al. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.04.028 · Cited by 85 · see citing works

Coiled-coil networking shapes cell molecular machinery

Wang, Y., Zhang, X., Zhang, H., Lu, Y., Huang, H., Dong, X., Chen, J., Dong, J., Yang, X., Hang, H., et al. (2012) · Molecular Biology of the Cell · doi:10.1091/mbc.e12-05-0396 · Cited by 83 · see citing works

Molecular requirements for the formation of a kinetochore–microtubule interface by Dam1 and Ndc80 complexes

Lampert, F., Mieck, C., Alushin, G. M., et al. (2012) · The Journal of Cell Biology · doi:10.1083/jcb.201210091 · Cited by 80 · see citing works

Conserved and divergent features of kinetochores and spindle microtubule ends from five species

McIntosh, J. R., O'Toole, E. T., Zhudenkov, K., et al. (2013) · The Journal of Cell Biology · doi:10.1083/jcb.201209154 · Cited by 78 · see citing works

Anaphase A: Disassembling Microtubules Move Chromosomes toward Spindle Poles

Asbury, C. L. (2017) · Biology · doi:10.3390/biology6010015 · Cited by 72 · see citing works

Chromatin Signaling to Kinetochores: Transregulation of Dam1 Methylation by Histone H2B Ubiquitination

Latham, J. A., Chosed, R. J., Wang, S., & Dent, S. (2011) · Cell · doi:10.1016/j.cell.2011.07.025 · Cited by 71 · see citing works

Dephosphorylation of the Ndc80 Tail Stabilizes Kinetochore-Microtubule Attachments via the Ska Complex

Cheerambathur, D. K., Prevo, B., Hattersley, N., et al. (2017) · Developmental Cell · doi:10.1016/j.devcel.2017.04.013 · Cited by 63 · see citing works

Assembling the Protein Architecture of the Budding Yeast Kinetochore-Microtubule Attachment using FRET

Aravamudhan, P., Felzer-Kim, I. T., Gurunathan, K., et al. (2014) · Current Biology · doi:10.1016/j.cub.2014.05.014 · Cited by 57 · see citing works

Conserved Tetramer Junction in the Kinetochore Ndc80 Complex

Valverde, R., Ingram, J. R., & Harrison, S. C. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.10.065 · Cited by 57 · see citing works

CCAN Assembly Configures Composite Binding Interfaces to Promote Cross-Linking of Ndc80 Complexes at the Kinetochore

Altunkaya, G. P., Malvezzi, F., Demianová, Z., et al. (2016) · Current Biology · doi:10.1016/j.cub.2016.07.005 · Cited by 56 · see citing works

Protein Arms in the Kinetochore-Microtubule Interface of the Yeast DASH Complex

Miranda, J. L., King, D. S., & Harrison, S. C. (2007) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-02-0135 · Cited by 53 · see citing works

Mechanism of Ska Recruitment by Ndc80 Complexes to Kinetochores

Janczyk, P. Ł., Skorupka, K. A., Tooley, J. G., Matson, D. R., Kestner, C. A., West, T. J., Pornillos, O., & Stukenberg, P. T. (2017) · Developmental Cell · doi:10.1016/j.devcel.2017.04.020 · Cited by 53 · see citing works

Kinetochores’ gripping feat: conformational wave or biased diffusion?

Asbury, C. L., Tien, J. F., & Davis, T. N. (2010) · Trends in Cell Biology · doi:10.1016/j.tcb.2010.09.003 · Cited by 51 · see citing works

The Budding Yeast Point Centromere Associates with Two Cse4 Molecules during Mitosis

Aravamudhan, P., Felzer-Kim, I. T., & Joglekar, A. P. (2013) · Current Biology · doi:10.1016/j.cub.2013.03.042 · Cited by 47 · see citing works

The Ndc80 complex bridges two Dam1 complex rings

Kim, J. O., Zelter, A., Umbreit, N. T., Bollozos, A., Riffle, M. E., Johnson, R. S., MacCoss, M. J., Asbury, C. L., & Davis, T. N. (2017) · eLife · doi:10.7554/elife.21069 · Cited by 47 · see citing works

The Dam1 ring binds to the E-hook of tubulin and diffuses along the microtubule

Ramey, V. H., Wang, H., Nakajima, Y., et al. (2010) · Molecular Biology of the Cell · doi:10.1091/mbc.e10-10-0841 · Cited by 45 · see citing works

The molecular architecture of the Dam1 kinetochore complex is defined by cross-linking based structural modelling

Zelter, A., Bonomi, M., Kim, J. O., Umbreit, N. T., Hoopmann, M. R., Johnson, R. S., Riffle, M. E., Jaschob, D., MacCoss, M. J., Moritz, R. L., et al. (2015) · Nature Communications · doi:10.1038/ncomms9673 · Cited by 44 · see citing works

Unique Phylogenetic Distributions of the Ska and Dam1 Complexes Support Functional Analogy and Suggest Multiple Parallel Displacements of Ska by Dam1

van Hooff, J. J. E., Snel, ‎., & Kops, G. J. P. L. (2017) · Genome Biology and Evolution · doi:10.1093/gbe/evx088 · Cited by 42 · see citing works

Real-space processing of helical filaments in SPARX

Behrmann, E., Tao, G., Stokes, D. L., et al. (2012) · Journal of Structural Biology · doi:10.1016/j.jsb.2011.12.020 · Cited by 34 · see citing works

Subunit organization in the Dam1 kinetochore complex and its ring around microtubules

Ramey, V. H., Wong, A., Fang, J., et al. (2011) · Molecular Biology of the Cell · doi:10.1091/mbc.e11-07-0659 · Cited by 26 · see citing works

Molecular architecture of the Dam1 complex–microtubule interaction

Legal, T., Zou, J., Sochaj, A. M., et al. (2016) · Open Biology · doi:10.1098/rsob.150237 · Cited by 25 · see citing works

The challenge of determining handedness in electron tomography and the use of DNA origami gold nanoparticle helices as molecular standards

Briegel, A., Pilhofer, M., Mastronarde, D. N., et al. (2013) · Journal of Structural Biology · doi:10.1016/j.jsb.2013.04.008 · Cited by 19 · see citing works

Tight-binding repressors of the lac operon: selection system and in vitro analysis

Pfahl, M. (1979) · Journal of Bacteriology · doi:10.1128/jb.137.1.137-145.1979 · Cited by 17 · see citing works

Mapping of I gene mutations which lead to repressors with increased affinity for lac operator

Pfahl, M. (1981) · Journal of Molecular Biology · doi:10.1016/0022-2836(81)90084-x · Cited by 14 · see citing works

Effect of DNA denaturants on the lac repressor-operator interaction

Pfahl, M. (1978) · Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis · doi:10.1016/0005-2787(78)90227-7 · Cited by 13 · see citing works

Exhaustive identification of interaction domains using a high-throughput method based on two-hybrid screening and PCR-convergence: molecular dissection of a kinetochore subunit Spc34p

Ikeuchi, A. (2003) · Nucleic Acids Research · doi:10.1093/nar/gkg888 · Cited by 10 · see citing works

A method for reverse interactome analysis: High‐resolution mapping of interdomain interaction network in Dam1 complex and its specific disorganization based on the interaction domain expression

Ikeuchi, A., Nakano, H., Kamiya, T., Yamané, T., & Kawarasaki, Y. (2010) · Biotechnology Progress · doi:10.1002/btpr.403 · Cited by 10 · see citing works

Molecular Structures of Yeast Kinetochore Subcomplexes and Their Roles in Chromosome SegregationPreprint

Jenni, S., Dimitrova, Y. N., Valverde, R., Hinshaw, S. M., & Harrison, S. C. (2017) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.2017.82.033738 · Cited by 7 · see citing works

Computed structures of core eukaryotic protein complexes

Humphreys, I. R., Pei, J., Baek, M., Krishnakumar, A., Anishchenko, I., Ovchinnikov, S., Zhang, J., Ness, T. J., Banjade, S., Bagde, S. R., et al. (2021) · Science · doi:10.1126/science.abm4805 · Cited by 542 · see citing works

Extensive loss of cell-cycle and DNA repair genes in an ancient lineage of bipolar budding yeasts

Steenwyk, J. L., Opulente, D. A., Kominek, J., Shen, X.-X., Zhou, X., Labella, A. L., Bradley, N. P., Eichman, B. F., Čadež, N., Libkind, D., et al. (2019) · PLoS Biology · doi:10.1371/journal.pbio.3000255 · Cited by 162 · see citing works

The plant kinetochore

Yu, H.-G., Dawe, R. K., Hiatt, E. N., & Dawe, R. K. (2000) · Trends in Plant Science · doi:10.1016/s1360-1385(00)01789-1 · Cited by 59 · see citing works

Seeing is believing: our evolving view of kinetochore structure, composition, and assembly

Hamilton, G. E., Dimitrova, Y. N., & Davis, T. N. (2019) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2019.03.016 · Cited by 21 · see citing works

Advance in the Research of Human Chromosome Kinetochore Proteins

Jing-hai, W. (2006)

The Ndc80 internal loop is required for recruitment of the Ska complex to establish end-on microtubule attachment to kinetochores.

Zhang, G., Kelstrup, C. D., Hu, X.-W., Hansen, M. J. K., Singleton, M. R., Olsen, J. V., & Nilsson, J. (2012) · Journal of Cell Science · doi:10.1242/jcs.104208 · Cited by 68 · see citing works

Stu1 inversely regulates kinetochore capture and spindle stabilityPreprint

Ortiz, J., Funk, C., Schäfer, A., & Lechner, J. (2009) · Genes & Development · doi:10.1101/gad.541309 · Cited by 27 · see citing works