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The mechanisms by which p38MAPK and HSP27 lead to keratinocyte dissociation are largely unclear but may involve reorganization of the keratinocyte cytoskeleton.
Our proposed regulatory model does not involve reorganization of the D1-D2 domainteractionion but requires flexibility in the linker between the transmembrane domain and the first D1 phosphatase domain.
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This involves reorganization of the cytoplasm and elimination of flagellar proteins in addition to PiCdc14.
Cell motility involves reorganization of the cell cytoskeleton, an intricate composite network of biopolymer filaments spanning the cell and endowing it with structure, mechanical stability, and function [1] [3].
This polarization process involves reorganization of the osteoclast cytoskeleton.
Cell migration and invasion of extracellular matrix beneath the basement membrane are essential steps involving reorganization of the actin cytoskeleton.
Furthermore, functional roles of genes that were differentially regulated imply that regulation involves reorganization of complexes at the ultrastructural level.
Moreover, activation of the dimer involves reorganization of hydrophobic regions of the EGFR [ 46]; nanoparticles obtained from dispersed PC at buffer pH 7.0 might favor such reorganization facilitating the formation of the active conformation.
Myofibroblast expansion occurs through the differentiation of fibroblasts [ 11]; this involves reorganization of the actin cytoskeleton, increased expression of alpha smooth muscle actin (αSMA) and incorporation of actin stress fibers [ 8].
The central thesis of this view is that evolutionary novelty often involves reorganization of preexisting phenotypes [ 9, 10] and this results in similarity of the novel changes among individuals, facilitates response to novel selection pressures, and can ultimately lead to genetic assimilation of the novel trait [ 9, 11- 16].
Various biological events involve physical reorganization of molecules to amplify the signal and trigger the downstream pathways.
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