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The finding that anchored kinases are refractory to active site inhibitors has important ramifications for drug discovery as endogenous binding partners that confer resistance to ATP analog inhibitors.
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There are binding partners that demonstrate preference for each of the known arrestin conformations: free, receptor-bound, and microtubule-bound.
These co-factors can have other binding partners that are themselves regulated by different signalling pathways.
There are no known binding partners that would interact with the periplasmic domain of AmtB.
Likely it requires binding partners that aid in vesicle nucleation, localization, targeting and recycling.
We identified p33ING1 as a binding partner that interacts with CSIG.
Many of these proteins arose out of hit-and-miss efforts to discover specific mutations, fusion partners or chemical modifications that confer desired properties.
This suggests that there are several putative binding sites for transcription factors that confer a negative effect on PGC-1α promoter activity.
MecA is the penicillin-binding protein that confers resistance to β-lactam antibiotics in MRSA strains.
The N-terminal portion of the β-subunit constitutes the heme-binding domain that confers NO sensitivity to the enzyme.
These genes encode RNA-binding proteins with chaperone activity that confer drought tolerance in maize and rice under field conditions.
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CEO of Professional Science Editing for Scientists @ prosciediting.com