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In addition, CD147 is capable of homotypic binding, which can lead to platelet degranulation upon platelet binding [ 21].
Therefore mutations can convert an Alu element into a dominant exon when completely removing hnRNP C binding, which can lead to disease.
Most antiparasitic agents targeting CYP51 are heme-iron coordinating compounds with potential to interact also with human CYPs, partially via nonspecific drug-metal binding, which can lead to various drug safety issues.
This causes an increase in the intensity of Nrf2-Maf transcomplexn complex formation and their strength of DNA binding, which can lead to uncontrolled antiapoptotic protein overexpression and consequently even to the process of carcinogenesis [ 62].
CD147 is capable of homotypic binding, which can lead to platelet degranulation upon platelet binding and stimulation of the nuclear factor kappa B (NF-κB) pathway in monocytes, which lead in turn to the production of matrix metalloproteinase (MMP) and cytokines, specifically MMP-9, TNF-α and IL-6 [ 20].
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Studies have shown that elevated insulin potentiates the activity of IGF-I either via direct upregulation or indirectly through the downregulation of IGF-binding protein 1 (34), which can lead to higher risk of lung cancer (35).
These observations indicated the presence and binding of proteins with AgNPs, which can lead to their possible stabilization and prevent agglomeration.
As an example of the coupling of multiple binding sites, Eph-ephrin binding may form hetero-tetramer or higher oligomers [ 11], which can lead to tighter cell adhesion.
The problems of nonspecific antibody binding (adsorption) (which requires the use of appropriate antibody isotype controls), low antibody sensitivity (which can lead to false negative results), and the presence of nonurothelial cells in the preparations can all lead to spurious results.
The authors of [ 33] used an extensive filtration procedure, which can lead to a high false negative rate, to limit their results to binding sites frequently occupied with Sp1.
E6 binding to zyxin, in a manner similar to paxillin, impairs the ability of these proteins to maintain proper cell structure, which can lead to cellular transformation.
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