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- W2033428498 abstract "Both kinesin and Rep face a similar problem—how to stay tightly associated with a linear polymer while still translocating rapidly and unidirectionally along it. While they have quite different structures and operate on different polymers, these enzymes appear to have evolved similar solutions to this problem. Both appear to use mechanisms in which one of the subunits of the dimer is tightly bound to the lattice while the second subunit moves forward to the next binding site. The two subunits then exchange identities and the process is repeated for further steps. The physical and biochemical evidence supporting this mechanism is convincing, but many important details remain to be deciphered. Importantly, the physical mechanism by which ATP hydrolysis is converted into forward motion and the nature of the intermediate in which the two subunits bind to the polymer and exchange identities are both poorly understood. It is likely that many other oligomeric motors operate using similar mechanisms, so understanding kinesin and Rep will hopefully provide molecular insight into many forms of intracellular motility." @default.
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- W2033428498 date "1998-04-01" @default.
- W2033428498 modified "2023-10-16" @default.
- W2033428498 title "Staying on Track: Common Features of DNA Helicases and Microtubule Motors" @default.
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- W2033428498 doi "https://doi.org/10.1016/s0092-8674(00)81139-3" @default.
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