1932

Abstract

▪ Abstract 

The genomics revolution has provided a deluge of new targets for drug discovery. To facilitate the drug discovery process, many researchers are turning to fragment-based approaches to find lead molecules more efficiently. One such method, Tethering1, allows for the identification of small-molecule fragments that bind to specific regions of a protein target. These fragments can then be elaborated, combined with other molecules, or combined with one another to provide high-affinity drug leads. In this review we describe the background and theory behind Tethering and discuss its use in identifying novel inhibitors for protein targets including interleukin-2 (IL-2), thymidylate synthase (TS), protein tyrosine phosphatase 1B (PTP-1B), and caspases.

Loading

Article metrics loading...

/content/journals/10.1146/annurev.biophys.33.110502.140409
2004-06-09
2024-10-08
Loading full text...

Full text loading...

/content/journals/10.1146/annurev.biophys.33.110502.140409
Loading
/content/journals/10.1146/annurev.biophys.33.110502.140409
Loading

Data & Media loading...

  • Article Type: Review Article
This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error