Sentence examples for motility speed of from inspiring English sources

The motility speed of myosin molecules extracted from hydrogen peroxide treated fibers was significantly decreased (P <  0.05) from 1.04 to 0.84 μm s−1 (Fig. 1D).

Furthermore, the high-content screening assay showed the motility speed of SGC-7901-FOXO4 cells is significantly lower than SGC-7901-NC SGC-7901-NC SGC-7901-NC cellsly showed the motility speed of SGC-7901-FOXO4 cells is lower than SGC-7901-NC cells.

In the present study, after treatment with H2O2, the motility speed of myosin decreased dramatically, which is in agreement with results in aged subjects, implying the oxidative stress-induced modifications compromise the myosin function.

Motility speeds of many species exceed in situ vertical current velocities; this also allows diel migrational patterns and other motility-based behavior to persist.

This random motility function does not require intracellular RHAMM proteins and immobilized recombinant cell surface RHAMM isoform (70 kDa) added to RHAMM−/− CD44−/− fibroblasts is sufficient restore fibroblast motility speed to that of wild type or RHAMM-rescued fibroblasts [ 55].

However, PTMs in the motor domain were only observed in the IIx MyHC isoform, suggesting PTMs in the rod region contributed to the observed disordering of myosin filaments and the slowing of motility speed.

In cooled semen, nutraceutical treatment also increased (P <.05) total motility, speed, and membrane integrity of spermatozoa compared with the control.

It is proposed that these PTMs contribute to the disordered myosin molecule organization and the slowing of motility speed.

(ii) An aging-related slowing of motility speed was observed in both type I and IIa MyHC assays, but the force-generating capacity was unaffected by age, irrespective of MyHC isoform.

The effects of old age on the function of specific myosin isoforms extracted from single human muscle fiber segments, demonstrated a significant slowing of motility speed (P <  0.001) in old age in both type I and IIa myosin heavy chain (MyHC) isoforms.

Third, glycation of skeletal muscle myosin changed the structural property of the protein and reduced simultaneously the in vitro motility speed (Ramamurthy et al. 2001).