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Keywords:

  • actin depolymerization;
  • amphidinolides;
  • cytoskeleton proteins;
  • cytotoxicity;
  • drug discovery

Errors were introduced into two graphics in this paper during the typesetting process. The correct Figures 6 and 8 are given here.

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Figure 6. Back-folding of the lipid tails toward the head-group planes as a function of the distance (d) from the TMRs (averaged over 0.5 μs).

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Figure 8. Time evolution of conformational changes in the SNARE complexes during fusion. I) The tilt angle between the TMRs of syntaxin (Sx1A, residue 266–288) and synaptobrevin (Syb2, residue 95–116), which represents the magnitude of mechanical stress in the SNARE complex. The horizontal lines represent the average and standard deviation of the tilt angle obtained from the simulation of the SNARE (X-ray structure) embedded in a POPE membrane patch (lower) and two unfused vesicles (upper). II) The minimum contact distance (d) between equal TMRs in different SNARE complexes. A plateau in the minimum contact distance at ≈0.5 nm corresponds to homodimerization between the TMRs. Both TMR species are dimerized between 110–420 ns. Loss of dimerization is related to the onset of membrane rupture. The gray line represents the fusion pore radius. The horizontal lines represent the times of resp. the formation of the stalk, rupture of the IMI and fusion pore.

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