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This pressure could originate either from forces exerted by actin polymerization against the mitochondrial outer membrane (Korobova et al., 2013), or by myosin-II dimer mediated contraction of actin filaments lying between the ER and mitochondrial membranes (Hatch et al., 2014; Korobova et al., 2014), or by a concerted action of these two complementary mechanisms.
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Taken together, these results indicate that the bradykinin-mediated contraction of the pig iris sphincter muscle seems to be mediated primarily by the activation of the B2 receptor release of acetylcholine, noradrenaline and both cyclooxygenase-1 and -2 metabolites besides the release of leukotriene D4 and tromboxane A2 from the arachidonic acid pathway.
These results affirm that collagen crosslinking treatments can prevent cell-mediated contraction of CDM scaffolds.
The current study examined the hypothesis that collagen crosslinking techniques could inhibit cell-mediated contraction of CDM scaffolds.
An in vitro co-culture system was devised to evaluate the effect of UEC on (i) SMC-mediated contraction of BAM discs, and (ii) SMC invasiveness into BAM.
The goal of this work was to investigate in vitro tendon cell-mediated contraction of collagen glycosaminoglycan (GAG) matrices cross-linked using selected methods.
The overall aim of the present study was to develop and characterise a reinforced natural scaffold using fibrin, collagen and glycosaminoglycan (FCG), and to examine the cell-mediated contraction of this scaffold in comparison to fibrin gels.
Cell-mediated contraction of the matrices varied with cross-linking: the most compliant DHT and UV matrices contracted the most (60% reduction in matrix diameter) and stiffest EDAC matrices contracted the least (30% reduction in matrix diameter).
Cell-mediated contraction of the scaffold was observed, which could be limited by the additional use of 1-ethyl-3-3dimethyl aminopropyl carbodiimide (EDAC) crosslinking without suppressing cartilage-specific matrix accumulation within the construct.
Wnt3a decreased the proliferation of fibroblasts, but significantly increased cell migration as well as fibroblast-mediated contraction of a collagen lattice.
Furthermore, thrombin was not able to induce C2C12-mediated contraction of pure Col I gels.
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