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The selection strategy enables the design of specific nucleic acids (aptamers) against virtually any target molecule.
Antibody phage technology has greatly facilitated the isolation of good-quality monoclonal antibodies to virtually any target antigen.
DARPins are built based on the natural ankyrin repeat protein fold with randomized surface residue positions allowing specific binding to virtually any target protein.
In particular, the hammerhead ribozyme, by virtue of its small size and ability to be designed to cleave virtually any target RNA, has been widely touted for the therapy of both genetic and infectious diseases.
Successful selection of fully active scFvs was obtained, confirming the notion that combinatorial mutagenesis of few amino acid residues centrally located in the antigen-binding site is sufficient to provide binding specificities against virtually any target.
Their affinity and specificity for a given protein make it possible to isolate a ligand to virtually any target, and adjusting their bioavailability expands their clinical utility.
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The exclusive selectivity and easy application to virtually any therapeutic target including intracellular factors and transcription factors renders siRNA oligonucleotide applications very promising.
But over time more precise weapons allowed NATO to destroy virtually any major target it wanted at minimal risk to its pilots.
The ability to link oligos to enzymes, fluorescent probes, affinity tags, or any other component has made possible the detection or assay of virtually any genomic target in tissues, cells, or extracts.
DNAzymes can be designed to cleave virtually any RNA target by selecting appropriate flanking sequences [32], [33].
They have the remarkable ability to recognize virtually any foreign targets (the antigens) and bind to these with extraordinary affinity and specificity (Mian et al., 1991; Sliwkowski and Mellman, 2013).
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