title: Molecular motors: Dynein's gearbox.
abstract: A new optical trapping study shows that the stepsize of cytoplasmic dynein varies according to the applied force, suggesting that this motor can change gear. Complementary biochemical kinetic work on yeast dynein mutants hints at the allosteric mechanisms involved.
authors.affiliation: Molecular Motors Group, Marie Curie Research Institute, The Chart, Oxted, Surrey RH8 0TL, UK. r.cross@mcri.ac.uk
authors.forename: R A
authors.initials: RA
authors.lastname: Cross
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism; D001692:Biological Transport; D001696:Biomechanical Phenomena; D003593:Cytoplasm / Q000378:metabolism*; D004398:Dyneins / Q000378:metabolism / Q000502:physiology*; D008954:Models, Biological; D020409:Molecular Motor Proteins / Q000502:physiology*; D017434:Protein Structure, Tertiary / Q000502:physiology
chemical_list: D020409:Molecular Motor Proteins; D000255:Adenosine Triphosphate; D004398:Dyneins