The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
Structure and Functional Role of Dynein's Microtubule-Binding Domain
Open accessAbstract
Dynein motors move various cargos along microtubules within the cytoplasm and power the beating of cilia and flagella. An unusual feature of dynein is that its microtubule-binding domain (MTBD) is separated from its ring-shaped AAA+ adenosine triphosphatase (ATPase) domain by a 15-nanometer coiled-coil stalk. We report the crystal structure of the mouse cytoplasmic dynein MTBD and a portion of the coiled coil, which supports a mechanism by which the ATPase domain and MTBD may communicate through a shift in the heptad registry of the coiled coil. Surprisingly, functional data suggest that the MTBD, and not the ATPase domain, is the main determinant of the direction of dynein motility.
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The HAMP Domain Structure Implies Helix Rotation in Transmembrane Signaling
Hulko, M., Berndt, F., Gruber, M., Linder, J. U., Truffault, V., Schultz, A., Martin, J., Schultz, J. E., Lupas, A. N., & Coles, M. (2006) · Cell · doi:10.1016/j.cell.2006.06.058 · Cited by 416
The beginning of kinesin's force-generating cycle visualized at 9-Å resolution
Sindelar, C. V., & Downing, K. H. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200612090 · Cited by 139
Kikkawa, M., & Hirokawa, N. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601299 · Cited by 125
Cited by
Functions and mechanics of dynein motor proteins
Roberts, A. J., Kon, T., Knight, P. J., Sutoh, K., & Burgess, S. A. (2013) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3667 · Cited by 537
Poirier, K., Lebrun, N., Broix, L., Tian, G., Saillour, Y., Boscheron, C., Parrini, E., Valence, S., Pierre, B. S., Oger, M., et al. (2013) · Nature Genetics · doi:10.1038/ng.2613 · Cited by 494
Subramanian, R., Wilson-Kubalek, E. M., Arthur, C. P., Bick, M. J., Campbell, E. A., Darst, S. A., Milligan, R. A., & Kapoor, T. M. (2010) · Cell · doi:10.1016/j.cell.2010.07.012 · Cited by 301
Self-citationThe 2.8 Å crystal structure of the dynein motor domain
Kon, T., Oyama, T., Shimo-Kon, R., Imamula, K., Shima, T., Sutoh, K., & Kurisu, G. (2012) · Nature · doi:10.1038/nature10955 · Cited by 260
DYNC2H1 Mutations Cause Asphyxiating Thoracic Dystrophy and Short Rib-Polydactyly Syndrome, Type III
Dagoneau, N., Goulet, M., Geneviève, D., Sznajer, Y., Martinovic, J., Smithson, S., Huber, C., Baujat, G., Flori, E., Tecco, L., et al. (2009) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2009.04.016 · Cited by 255
Metadata
- Authors
- Carter, A. P., Garbarino, J. E., Wilson-Kubalek, E. M., Shipley, W. E., Cho, C., Milligan, R. A., Vale, R. D., & Gibbons, I. R.
- Venue
- Science
- Published
- 2008-12-12
- Volume
- 322
- Issue
- 5908
- Pages
- 1691-1695
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2064047527
- Cited by
- 248
- References
- 3
- FWCI
- 7.36
- Type
- journal article
- Language
- en
- Open access
- green
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- Carter, A. P., Garbarino, J. E., Wilson-Kubalek, E. M., Shipley, W. E., Cho, C., Milligan, R. A., Vale, R. D., & Gibbons, I. R. (2008). Structure and Functional Role of Dynein's Microtubule-Binding Domain. Science. https://doi.org/10.1126/science.1164424
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