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This is two-fold slower than the measured gliding velocity.
However, gliding velocity of T192 the cells is not significantly different from that exhibited by the WT cells.
We therefore postpone the added complexity involved with balancing forces and calculating the gliding velocity of the model cell.
To correlate the gliding velocity with ATP turnover, we determined the microtubule-activated steady state ATPase rate of Head3/Neck1.
Assuming a hand-over-hand mechanism with steps of 8 nm, this would lead to a gliding velocity of 0.19 µm/s, threefold lower than actually observed.
Probably, the slower gliding velocity of the cells from this mutant delays both separation of daughter cells and chromosome segregation increasing in this way the proportion of cells with a high DNA content.
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The microtubule gliding velocities of various mutants tested in this study (labels and scale bar are indicated).
Additionally, mixing WT with the E253K de novo mutant kinesin in the assays showed an approximately eightfold reduction in microtubule gliding velocities.
However, the V220I (polymorphism) and A255V (recessive) mutations exhibited microtubule gliding velocities similar to that of WT (Fig. 5, Table S2, Video S1).
This mixed motor surface showed a drastic reduction (∼eightfold) in gliding velocities compared to WT alone indicating that the E253K mutation might exert a dominant negative effect over WT KIF1A function in vivo.
Automated tracking of motors revealed a Gaussian velocity distribution of Cik1 Kar3 with a mean speed of 77 ± 23 nm/s (mean ± SD; Figure 2B) in range with reported microtubule gliding velocities for truncated Cik1 Kar3 molecules (Chu et al., 2005; Allingham et al., 2007).
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