The DOI matches its Crossref record; 13 of the 13 references it cites were found in a registry or an index.
Molecular Motors: A Theorist's Perspective
Abstract
Individual molecular motors, or motor proteins, are enzymatic molecules that convert chemical energy, typically obtained from the hydrolysis of ATP (adenosine triphosphate), into mechanical work and motion. Processive motor proteins, such as kinesin, dynein, and certain myosins, step unidirectionally along linear tracks, specifically microtubules and actin filaments, and play a crucial role in cellular transport processes, organization, and function. In this review some theoretical aspects of motor-protein dynamics are presented in the light of current experimental methods that enable the measurement of the biochemical and biomechanical properties on a single-molecule basis. After a brief discussion of continuum ratchet concepts, we focus on discrete kinetic and stochastic models that yield predictions for the mean velocity, V(F, [ATP], …), and other observables as a function of an imposed load force F, the ATP concentration, and other variables. The combination of appropriate theory with single-molecule observations should help uncover the mechanisms underlying motor-protein function.
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Citations
Cites
Mechanics of Motor Proteins and the Cytoskeleton
Howard, & Clark (2002) · Applied Mechanics Reviews · doi:10.1115/1.1451234 · Cited by 2,909
The Molecular Motor Toolbox for Intracellular Transport
Vale, R. D. (2003) · Cell · doi:10.1016/s0092-8674(03)00111-9 · Cited by 1,982
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
Carter, N. J., & Cross, R. A. (2005) · Nature · doi:10.1038/nature03528 · Cited by 743
Force production by single kinesin motors
Schnitzer, M. J., Visscher, K., & Block, S. M. (2000) · Nature Cell Biology · doi:10.1038/35036345 · Cited by 572
The Crystal Structure of Dimeric Kinesin and Implications for Microtubule-Dependent Motility
Kozielski, F., Sack, S., Marx, A., Thormählen, M., Schönbrunn, E., Biou, V, Thompson, A., Mandelkow, E.-M., & Mandelkow, E. (1997) · Cell · doi:10.1016/s0092-8674(00)80489-4 · Cited by 408
Kinesin Takes One 8-nm Step for Each ATP That It Hydrolyzes
Coy, D. L., Wagenbach, M., & Howard, J. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.6.3667 · Cited by 390
Coupling of kinesin steps to ATP hydrolysis
Hua, W., Young, E. C., Fleming, M. L., & Gelles, J. (1997) · Nature · doi:10.1038/41118 · Cited by 358
Chemomechanical coupling of the forward and backward steps of single kinesin molecules
Nishiyama, M., Higuchi, H., & Yanagida, T. (2002) · Nature Cell Biology · doi:10.1038/ncb857 · Cited by 327
Probing the kinesin reaction cycle with a 2D optical force clamp
Block, S. M., Asbury, C. L., Shaevitz, J. W., & Lang, M. J. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0436709100 · Cited by 295
Cited by
Stochastic thermodynamics, fluctuation theorems and molecular machines
Seifert, U. (2012) · Reports on Progress in Physics · doi:10.1088/0034-4885/75/12/126001 · Cited by 3,300
Dynamic personalities of proteins
Henzler-Wildman, K., & Kern, D. (2007) · Nature · doi:10.1038/nature06522 · Cited by 2,545
Recent Advances in Optical Tweezers
Moffitt, J. R., Chemla, Y. R., Smith, S. B., & Bustamante, C. (2008) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.77.043007.090225 · Cited by 1,084
Equalities and Inequalities: Irreversibility and the Second Law of Thermodynamics at the Nanoscale
Jarzynski, C. (2011) · Annual Review of Condensed Matter Physics · doi:10.1146/annurev-conmatphys-062910-140506 · Cited by 1,012
Thermodynamic Uncertainty Relation for Biomolecular Processes
Barato, A. C., & Seifert, U. (2015) · Physical Review Letters · doi:10.1103/physrevlett.114.158101 · Cited by 957
Metadata
- Authors
- Kolomeisky, A. B., & Fisher, M. E.
- Venue
- Annual Review of Physical Chemistry
- Publisher
- Annual Reviews
- Published
- 2007-05-01
- Volume
- 58
- Issue
- 1
- Pages
- 675-695
- ISSN
- 0066-426X (ISSN-L)
- 1545-1593
- OpenAlex
- W2166454051
- Cited by
- 575
- References
- 13
- FWCI
- 1.57
- Type
- journal article
- Language
- en
- Open access
- closed
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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).
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