Skip to main content

Thank you for visiting nature.com. You are using a browser version with limited support for CSS. To obtain the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles and JavaScript.

  • Research Highlights
  • Published:

To affinity and beyond

Nature Methods volume 2, page 243 (2005)Cite this article

Abstract

A quick, sensitive screen for identifying the binding preferences of protein kinases for various compounds has made it possible to assemble detailed interaction maps, with initial data revealing surprising and important ramifications for drug design.

This is a preview of subscription content, access via your institution

Access options

Buy this article

  • Purchase on SpringerLink
  • Instant access to the full article PDF.

USD 39.95

Prices may be subject to local taxes which are calculated during checkout

Figure 1: Profiles of three kinase inhibitors.

References

  1. Fabian, M.A. et al. A small molecule–kinase interaction map for clinical kinase inhibitors. Nat. Biotechnol. 23, 329–336 (2005).

    Article  CAS  Google Scholar 

  2. Manning, G. et al. The protein kinase complement of the human genome. Science 298, 1912–1934 (2002).

    Article  CAS  Google Scholar 

Download references

Authors
  1. Michael Eisenstein
    View author publications

    Search author on:PubMed Google Scholar

Rights and permissions

Reprints and permissions

About this article

Cite this article

Eisenstein, M. To affinity and beyond. Nat Methods 2, 243 (2005). https://doi.org/10.1038/nmeth0405-243

Download citation

  • Issue date:

  • DOI: https://doi.org/10.1038/nmeth0405-243

Search

Advanced search

Quick links

Nature Briefing

Sign up for the Nature Briefing newsletter — what matters in science, free to your inbox daily.

Get the most important science stories of the day, free in your inbox. Sign up for Nature Briefing