The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
A Conserved Mechanism for Centromeric Nucleosome Recognition by Centromere Protein CENP-C
Open accessAbstract
Kinetochore Targeting: Chromosomes must be segregated accurately during cell division. This is facilitated by the attachment of mitotic spindle microtubules to the kinetochore at the chromosomal centromere. The centromere is marked with the histone H3 variant CenH3 (CENP-A in human), and CENP-C forms part of the inner kinetochore. Kato et al. (p. 1110 ) used structural biology, biochemistry, and mutagenesis to show that CENP-C recognizes CENP-A chromatin via several different interactions. The CENP-C "central domain" makes close contact with the acidic patch of histones H2A/H2B, and the highly conserved "CENP-C motif" senses both the acidic patch and recognizes the hydrophobicity of the otherwise nonconserved CenH3 tail, supporting a conserved mechanism of centromere targeting by the kinetochore.
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PHENIX : 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
Phaser crystallographic software
McCoy, A. J., Grosse-Kunstleve, R. W., Adams, P. D., Winn, M. D., Storoni, L. C., & Read, R. J. (2007) · Journal of Applied Crystallography · doi:10.1107/s0021889807021206 · Cited by 20,612
Kabsch, W. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909047337 · Cited by 16,463
MolProbity : 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
HADDOCK: A Protein−Protein Docking Approach Based on Biochemical or Biophysical Information
Dominguez, C., Boelens, R., & Bonvin, A. M. J. J. (2003) · Journal of the American Chemical Society · doi:10.1021/ja026939x · Cited by 3,187
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Structure of the human inner kinetochore bound to a centromeric CENP-A nucleosome
Yatskevich, S., Muir, K. W., Bellini, D., Zhang, Z., Yang, J., Tischer, T., Predin, M., Dendooven, T., McLaughlin, S. H., & Barford, D. (2022) · Science · doi:10.1126/science.abn3810 · Cited by 120
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Dudziak, A., Pleuger, R., Schmidt, J., Hamm, F., Tendulkar, S., Jänen, K., Vetter, I. R., Singh, S., Fischböck, J., Herzog, F., et al. (2025) · The EMBO Journal · doi:10.1038/s44318-025-00437-w · Cited by 4
Insects evolved a monomeric histone-fold domain in the CENP-T protein family
Sankaranarayanan, S. R., Ulmer, J., Mørch, A., Ali-Ahmad, A., Sekulić, N., & Drinnenberg, I. A. (2025) · EMBO Reports · doi:10.1038/s44319-025-00603-5 · Cited by 2
Metadata
- Authors
- Kato, H., Jiang, J., Zhou, B.-R., Rozendaal, M., Feng, H., Ghirlando, R., Xiao, T. S., Straight, A. F., & Bai, Y.
- Venue
- Science
- Published
- 2013-05-31
- Volume
- 340
- Issue
- 6136
- Pages
- 1110-1113
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2145579024
- Cited by
- 323
- References
- 5
- FWCI
- 15.97
- Type
- journal article
- Language
- en
- Open access
- green
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- Kato, H., Jiang, J., Zhou, B.-R., Rozendaal, M., Feng, H., Ghirlando, R., Xiao, T. S., Straight, A. F., & Bai, Y. (2013). A Conserved Mechanism for Centromeric Nucleosome Recognition by Centromere Protein CENP-C. Science. https://doi.org/10.1126/science.1235532
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