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Proteoglycans (PGs) exhibit a crucial role for matrix assembly and remodeling.
These may be used in the matrix assembly and internal point calculations.
As forces operate against tissues they establish tissue architecture, extracellular matrix assembly, and pattern cell shapes.
Because conventional FEM solvers do not consider the frequent changes in the geometrical boundary conditions, efficient matrix assembly and matrix rearrangement have not attracted much attention.
Through integrin engagement with ECM components and cytoskeletal contractility, myofibroblasts exert large forces on the ECM thus enabling matrix assembly and alignment [24].
This paper focuses on parallel algorithms for matrix assembly and matrix rearrangement related to FEM procedures by considering a sparse-matrix storage format.
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Agonist stimulation leads cells to regulate integrin affinity ("activation"), thus controlling cell adhesion and migration, controlling extracellular-matrix assembly, and contributing to angiogenesis, tumor cell metastasis, inflammation, the immune response, and hemostasis.
Many mechanisms are involved to regulate FN-matrix assembly, and there is now also growing evidence that in addition to regulation via molecules, the ECM composition and structure itself are also important.
Glycosaminoglycans (GAGs) are ubiquitously present at the cell surface and in extracellular matrix, and crucial for matrix assembly, cell cell and cell-matrix interactions.
This soluble protein is involved in a number of cellular processes including matrix assembly, fibrillogenesis, and the control of cell proliferation [18], [24] [33].
The strict correlation between the luminal matrix assembly defects and the tube expansion phenotypes strongly suggest that the swelling luminal matrixes directly enlarge the tubes from the inside (Figure 7E).
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