1994
DOI: 10.1038/372515a0
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Abstract: What is the molecular basis of cell movement and changes in cell shape? The integration of three approaches is revealing how the molecular motors that drive these processes move and produce force.

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Cited by 441 publications
(329 citation statements)
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“…Similarly, tachyzoites treated with jasplakinolide, a membrane-permeable actin-polymerizing and filament-stabilizing drug, reversibly inhibit host cell invasion (Shaw and Tilney, 1999). Members of the myosin superfamily are mechanoenzymes that convert chemical energy stored in ATP into a directed force along actin filaments (Spudich, 1994). In the past few years evidence has emerged for roles played by actin-based molecular motors in a wide range of membrane movements (Hasson and Mooseker, 1995;Mermall et al, 1998).…”
Section: Introductionmentioning
confidence: 99%
“…Similarly, tachyzoites treated with jasplakinolide, a membrane-permeable actin-polymerizing and filament-stabilizing drug, reversibly inhibit host cell invasion (Shaw and Tilney, 1999). Members of the myosin superfamily are mechanoenzymes that convert chemical energy stored in ATP into a directed force along actin filaments (Spudich, 1994). In the past few years evidence has emerged for roles played by actin-based molecular motors in a wide range of membrane movements (Hasson and Mooseker, 1995;Mermall et al, 1998).…”
Section: Introductionmentioning
confidence: 99%
“…This increase of ionic concentration originates conformational changes in the troponin-tropomyosin complex and consequently the muscular contraction. All these processes occur in aqueous medium and at constant temperature [1][2][3]81]. A sketch of the mechanism is shown in ref.…”
Section: Similarities With Natural Musclesmentioning
confidence: 99%
“…Taking into account the nature and the operation of its perfect machines, a material is required capable to conduct ions and electrons [1][2][3][4]. It should be able to work with electric pulses in the mV region (natural muscles use a potential ≈ 175 mV), it should experience a volume variation associated with conformational changes in its structure.…”
Section: Introductionmentioning
confidence: 99%
“…Because of their flexibility, two surface loops were not resolved. These loops are located at the actin contact interface (loop 2) and over the "mouth" of the ATP binding pocket (loop 1) and proposed to modulate actin-binding and exchange of ATP and its hydrolysis products, respectively (42). Another structural characteristic of most myosin motor domains is the presence of a negatively charged residue at a very precise position, shown to be crucial for activity.…”
Section: Myosins Are Tripartite Modular Motorsmentioning
confidence: 99%