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We demonstrate that this method is feasible by preparing small inhibitor for human immunodeficiency virus infection.
These investigations would lead to the development of effective anti-biofilm therapies and technologies that would target specific or multiple ECM components using different enzymes or small inhibitor compounds.
Thus, down regulation of excessive KLK activity in cancer and in skin diseases by small inhibitor compounds may represent attractive therapeutical approaches.
Structures and associated Ki values for a lead inhibitor (CA-11) bound to uPA and to five other proteases, as well as for other leads bound to multiple proteases, help reveal the features responsible for the potency (Ki=11 nM) and selectivity of the remarkably small inhibitor, CA-11.
To achieve binding specificity and targeting ability, QDs can be linked to monoclonal antibodies, peptides, oligonucleotides, small inhibitor or hydrophilic segment (such as polyethylene glycol [PEG]).
With the availability of technologies for large scale screening, design and development specific small inhibitor molecules for specific DUBs is required and will be helpful for the generation of novel cancer therapeutics.
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Moreover, selective small inhibitors disrupting the protein protein interactions involved in the MYC signaling network have been developed.
However, blocking the enzymatic activity with synthetic small inhibitors appears to be an extremely difficult task.
Taken together, this study provides a structural basis for designing small inhibitors to control locust.
One strategy to design small inhibitors of STAT3 dimerization, consists in using phosphotyrosine-based peptidomimetics targeted to the SH2 domain.
We have designed novel small inhibitors of rabbit 20S proteasome using a trifluoromethyl-β-hydrazino acid scaffold.
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