The DOI matches its Crossref record; 27 of the 27 references it cites were found in a registry or an index.
Insight into tubulin regulation from a complex with colchicine and a stathmin-like domain
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Citations
Cites
The CCP4 suite: programs for protein crystallography
Collaborative Computational Project, N. 4. (1994) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444994003112 · Cited by 17,270
Use of TLS parameters to model anisotropic displacements in macromolecular refinement
Winn, M. D., Isupov, M. N., & Murshudov, G. N. (2001) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444900014736 · Cited by 1,696
High-Resolution Model of the Microtubule
Nogales, E., Whittaker, M., Milligan, R. A., & Downing, K. H. (1999) · Cell · doi:10.1016/s0092-8674(00)80961-7 · Cited by 1,195
Colchicine-binding protein of mammalian brain and its relation to microtubules
Weisenberg, R. C., Broisy, G. G., & Taylor, E. W. (1968) · Biochemistry · doi:10.1021/bi00852a043 · Cited by 1,158
Refined structure of αβ-tubulin at 3.5 Å resolution 1 1Edited by I. A. Wilson
Löwe, J., Li, H., Downing, K. H., & Nogales, E. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.5077 · Cited by 1,145
Crystal structure of the bacterial cell-division protein FtsZ
Löwe, J., & Amos, L. A. (1998) · Nature · doi:10.1038/34472 · Cited by 906
Belmont, L. D., & Mitchison, T. J. (1996) · Cell · doi:10.1016/s0092-8674(00)81037-5 · Cited by 663
Tubulin and FtsZ form a distinct family of GTPases
Nogales, E., Downing, K. H., Amos, L. A., & L�we, J. (1998) · Nature Structural Biology · doi:10.1038/nsb0698-451 · Cited by 613
The oncoprotein 18/stathmin family of microtubule destabilizers
Cassimeris, L. (2002) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(01)00289-7 · Cited by 432
Microtubule Structure at 8 Å Resolution
Li, H., DeRosier, D. J., Nicholson, W. V., Nogales, E., & Downing, K. H. (2002) · Structure · doi:10.1016/s0969-2126(02)00827-4 · Cited by 413
Cited by
Efficacy and safety of low-dose colchicine after myocardial infarction
Tardif, J.-C., Kouz, S., Waters, D. D., Bertrand, O. F., Diaz, R., Maggioni, A. P., Pinto, F. J., Ibrahim, R., Gamra, H., Kiwan, G. S., et al. (2019) · New England Journal of Medicine · doi:10.1056/nejmoa1912388 · Cited by 3,159
Control of microtubule organization and dynamics: Two ends in the limelight
Akhmanova, A., & Steinmetz, M. O. (2015) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm4084 · Cited by 895
An overview of tubulin inhibitors that interact with the colchicine binding site
Lu, Y., Chen, J., Xiao, M., Li, W., & Miller, D. D. (2012) · Pharmaceutical Research · doi:10.1007/s11095-012-0828-z · Cited by 709
Alushin, G. M., Lander, G. C., Kellogg, E. H., Zhang, R., Baker, D., & Nogales, E. (2014) · Cell · doi:10.1016/j.cell.2014.03.053 · Cited by 696
Tau stabilizes microtubules by binding at the interface between tubulin heterodimers
Kadavath, H., Hofele, R. V., Biernat, J., Kumar, S., Tepper, K., Urlaub, H., Mandelkow, E., & Zweckstetter, M. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1504081112 · Cited by 524
Metadata
- Authors
- Ravelli, R. B. G., Gigant, B., Curmi, P. A., Jourdain, I., Lachkar, S., Sobel, A., & Knossow, M.
- Venue
- Nature
- Published
- 2004-03
- Volume
- 428
- Issue
- 6979
- Pages
- 198-202
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2064571598
- Cited by
- 1,630
- References
- 27
- FWCI
- 15.43
- Type
- journal article
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: Insight into tubulin regulation from a complex with colchicine and a stathmin-like domain. https://app.cochat.ai/papers/10.1038/nature02393
- The paper
- Ravelli, R. B. G., Gigant, B., Curmi, P. A., Jourdain, I., Lachkar, S., Sobel, A., & Knossow, M. (2004). Insight into tubulin regulation from a complex with colchicine and a stathmin-like domain. Nature. https://doi.org/10.1038/nature02393
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.