The DOI matches its Crossref record; 10 of the 10 references it cites were found in a registry or an index.
The Movement of Kinesin Along Microtubules
Abstract
The molecular motor kinesin is a homodimer containing two heads-globular domains each of which has an ATP- and a microtubule-binding site. It is argued by analogy to other proteins with coiled-coil dimerization domains that the kinesin dimer has an approximate axis of rotational symmetry. The path kinesin follows along the surface of the microtubule is parallel to the protofilaments, and the steps are likely separated by 8 nm, the length of the tubulin dimer. Micromechanical recordings from single kinesin molecules indicate that one motor can exert a force as great as 5 pN. The efficiency of kinesin probably is in the order of 50%, considering the free energy available from ATP hydrolysis. Structural, mechanical, and biochemical experiments suggest that in order not to let go of a microtubule, the two heads of kinesin might move in a coordinated manner, perhaps undergoing a rotary motion.
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Cites
Predicting coiled coils from protein sequences.
Lupas, A., Van Dyke, M., & Stock, J. (1991) · Science · doi:10.1126/science.252.5009.1162 · Cited by 3,953
Identification of a novel force-generating protein, kinesin, involved in microtubule-based motility
VALE, R., REESE, T., & SHEETZ, M. (1985) · Cell · doi:10.1016/s0092-8674(85)80099-4 · Cited by 1,993
Direct observation of kinesin stepping by optical trapping interferometry
Svoboda, K., Schmidt, C. F., Schnapp, B. J., & Block, S. M. (1993) · Nature · doi:10.1038/365721a0 · Cited by 1,910
The packing of α-helices: simple coiled-coils
Crick, F. H. C. (1953) · Acta Crystallographica · doi:10.1107/s0365110x53001964 · Cited by 1,578
Bead movement by single kinesin molecules studied with optical tweezers
Block, S. M., Goldstein, L. S. B., & Schnapp, B. J. (1990) · Nature · doi:10.1038/348348a0 · Cited by 1,038
Force and velocity measured for single kinesin molecules
Svoboda, K., & Block, S. M. (1994) · Cell · doi:10.1016/0092-8674(94)90060-4 · Cited by 909
Hirokawa, N., Pfister, K. K., Yorifuji, H., Wagner, M. C., Brady, S. T., & Bloom, G. S. (1989) · Cell · doi:10.1016/0092-8674(89)90691-0 · Cited by 477
Stewart, R. J., Thaler, J. P., & Goldstein, L. S. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.11.5209 · Cited by 145
The Drosophila kinesin light chain. Primary structure and interaction with kinesin heavy chain
Gauger, A. K., & Goldstein, L. S. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)38698-3 · Cited by 105
Kuznetsov, S. A., Vaisberg, Y. A., Rothwell, S. W., Murphy, D. B., & Gelfand, V. I. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)31301-7 · Cited by 95
Cited by
Brownian motors: noisy transport far from equilibrium
Reimann, P. (2002) · Physics Reports · doi:10.1016/s0370-1573(01)00081-3 · Cited by 2,589
Single kinesin molecules studied with a molecular force clamp
Visscher, K., Schnitzer, M. J., & Block, S. M. (1999) · Nature · doi:10.1038/22146 · Cited by 1,027
Kinbara, K., & Aida, T. (2005) · Chemical Reviews · doi:10.1021/cr030071r · Cited by 865
Kinesin hydrolyses one ATP per 8-nm step
Schnitzer, M. J., & Block, S. M. (1997) · Nature · doi:10.1038/41111 · Cited by 771
Kinesin Moves by an Asymmetric Hand-Over-Hand Mechanism
Asbury, C. L., Fehr, A. N., & Block, S. M. (2003) · Science · doi:10.1126/science.1092985 · Cited by 511
Metadata
- Authors
- Howard, J.
- Venue
- Annual Review of Physiology
- Publisher
- Annual Reviews
- Published
- 1996-10
- Volume
- 58
- Issue
- 1
- Pages
- 703-729
- ISSN
- 0066-4278 (ISSN-L)
- 1545-1585
- OpenAlex
- W2175246397
- Cited by
- 246
- References
- 10
- FWCI
- 6.56
- Type
- journal article
- Language
- en
- Open access
- closed
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- Howard, J. (1996). The Movement of Kinesin Along Microtubules. Annual Review of Physiology. https://doi.org/10.1146/annurev.ph.58.030196.003415
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.
