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Systematic swapping of modular protein domains verifies a mechanism for generation of phenotypic diversity in yeast.
Toward this goal, modular protein polymer-based hydrogels were created through genetic engineering and enzymatic crosslinking.
Src-homology (SH3) domain belongs to a class of ubiquitous modular protein domains found in nature.
These results clearly establish CAR as a xenobiotic responsive modular protein that can be activated/deactivated by binding with agonistic and antagonistic ligands, respectively.
These studies demonstrate that primitive vessel networks can be formed by modular protein microbeads containing embedded endothelial cells and fibroblasts.
Nonribosomal peptide synthetases (NRPSs) are large modular protein templates that assemble bioactive peptides, many of which possess therapeutic importance.
The Src homology domains SH2 and SH3 are small modular protein motifs about 100 and 60 amino acids long, respectively.
Downing proposed to study the structure of fibrillin 1, a large cell-membrane modular protein, and to examine how structural changes in the protein relate to human disease.
In this study, modular protein microbeads were prepared from pure fibrin (FIB) and collagen fibrin composites (COL FIB) using a simple water-in-oil emulsification technique.
Specifically, we use a biomimetic engineered extracellular matrix (eECM) that contains modular protein domains derived from two ECM proteins found in the small intestine, fibronectin and elastin.
Tenascin-C (TNC) is an ECM tandem modular protein and plays an important role in mechanotransduction by regulating important cell matrix interactions.
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