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Furthermore, adhesion of basal epithelial cells to the extracellular matrix is mediated by several classes of receptor, the most extensively characterized being integrins.
Previously, it has been suggested that PP IX accumulation in the mitochondrial matrix is mediated by the PPO/FECH transmembrane complex.
Adhesion of actin network through plasma membrane to the extracellular matrix is mediated by specialized protein complexes termed focal adhesions (FAs) [3] [5], which also serve as signal transduction sites where the cell gathers information about the mechanical and chemical properties of the environment [3], [6].
Sequestration of TG2 into the pericellular matrix is mediated by fibronectin (FN) binding (Gaudry et al. 1999a; Scarpellini et al. 2009).
Adhesion of EOC cells to collagen types I and III in the submesothelial matrix is mediated by α2β1 and α3β1 integrins [ 14– 16].
Adhesion of cells to the extracellular matrix is mediated through the integrin family of cell-surface receptors and leads to the activation of multiple biological responses, including calcium influx, increased protein tyrosine phosphorylation and activation of MAPK cascade [ 55].
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Our next experiment was designated to evaluate whether VEGF-induced formation of capillary/tube-like networks in a type I collagen gel matrix was mediated by ILK.
Turnover of the extracellular matrix (ECM) is mediated by matrix metalloproteinases (MMPs), a family of at least 24 zinc-dependent endopeptidases.
Normal development of the facial primordia requires remodelling of the extracellular matrix, which is mediated in part by the matrix metalloproteinases (MMPs).
The movement of most charged metabolites into the matrix space is mediated by special carrier proteins in the crista that catalyze exchange-diffusion (i.e., a one-for-one exchange).
During life, cartilage matrix turnover is mediated by a multitude of complex autocrine and paracrine anabolic and catabolic factors.
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