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The action of cholera toxin and E. coli heat-labile enterotoxin can be inhibited by blocking their binding to the cell-surface receptor GM1.
These compounds act by binding the bromodomain of the BET family of proteins, blocking their binding to acetyl-lysine residues and inhibiting activation of gene transcription.
Several reports suggest that the position of the nucleosome is critical in globally regulating the in vivo binding of transcription factors by either allowing or blocking their binding to the nucleosome [ 5- 9].
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We have also determined that the mechanism by which this occurs is through inhibition of GF- and cytokine-stimulated STAT3/ and STAT5/receptor binding thus blocking their recruitment to the plasma membrane.
Further, the bispecific antibodies were comparable to their parent antibodies in their potency in blocking ligand binding to the receptors and in inhibiting ligand-induced biological activities.
These secreted proteins are present in the extracellular space and alter the activities of the ligands by binding to and blocking their interaction with their cellular receptors, thereby essentially decreasing the concentration of the "free" ligand.
TIMPs work by binding to MMPs thereby blocking their activity.
Also, Chordin antagonizes signaling by bone morphogenetic proteins (BMPs) by blocking binding to their receptors.
TAM acts by blocking estrogen binding to its receptor, while AIs block estrogen production [ 8].
The compounds were tested for their ability to block CTB5 binding to immobilized ganglioside receptor and compared to the two previous leads.
These compounds were purchased and tested for their ability to block Stat3 binding to its phosphopeptide ligand in a surface plasmon resonance (SPR -based binding aSPR -basedo inhibinding6-mediassayphosphorylandon of Stot3.
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