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It is encouraging that small molecules that promote cardiac differentiation are being identified from high throughput screens and from rational compound selection (Table 3).
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To implement the paradigm for structure-based drug design, we have developed a complex-binding modulation (CBM) algorithm for the rational design of compounds (CBM compounds) that can affect biomolecular interactions by binding to the intermolecular pockets or cavities of biomolecular complexes.
Our current work is expected to offer new insight into construction of dual separation channels for rational design and compound of photocatalyst with high performance.
Rational design of compounds from established modules can potentially yield compounds that bind strongly and selectively with specific DNA sequences.
Furthermore, using a rational approach 1697 compounds were selected for a focused kinase set which was subsequently expanded to 3885 compounds.
These compounds include ABT-737 and ABT-263, obatoclax, gossypol derivatives such as apogossypol, apogossypolone, and sabutoclax, other rational design-based compounds such as B-12 and BH3-M6, and the recently identified maritoclax.
However, there is no an available methodology for the rational design of compounds with anti-sarcoma activity.
Rational improvements to compounds of this class resulted in single-digit nanomolar enzyme and cellular activity against PLK1, and oral bioavailability.
The identification of CFTR activators and inhibitors with novel chemical scaffolds might help with the rational design of compounds with improved pharmacological properties.
Rational design of compounds to mimic the functional domains of BCL‐2 family proteins requires chemical reproduction of the biologic complexity afforded by the relatively large and folded surfaces of BCL‐2 homology (BH) domain peptide α‐helices.
The ability to efflux such a large number of drugs remains a biological enigma and the lack of mechanistic understanding of the translocation pathway used by P-gp prevents rational design of compounds to inhibit its function.
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