Jump to main content
Jump to site search

Issue 2, 2014
Previous Article Next Article

Fragment growing to retain or alter the selectivity of anchored kinase hinge-binding fragments

Author affiliations

Abstract

The activity patterns of kinase hinge-binding fragments can be retained or redirected in fragment growing strategies. Targeting conserved kinase features preserved the selectivity pattern of a PKB hinge-binding fragment over a 5000-fold increase in potency, while late-stage modification of a CHK1 hinge-binding fragment substantially changed the pattern.

Graphical abstract: Fragment growing to retain or alter the selectivity of anchored kinase hinge-binding fragments

Back to tab navigation

Supplementary files

Publication details

The article was received on 15 Oct 2013, accepted on 13 Dec 2013 and first published on 16 Dec 2013


Article type: Concise Article
DOI: 10.1039/C3MD00308F
Author version
available:
Download author version (PDF)
Citation: Med. Chem. Commun., 2014,5, 180-185
  • Open access: Creative Commons BY license
  •   Request permissions

    Fragment growing to retain or alter the selectivity of anchored kinase hinge-binding fragments

    C. E. Allen, A. J. Welford, T. P. Matthews, J. J. Caldwell and I. Collins, Med. Chem. Commun., 2014, 5, 180
    DOI: 10.1039/C3MD00308F

    This article is licensed under a Creative Commons Attribution 3.0 Unported Licence. Material from this article can be used in other publications provided that the correct acknowledgement is given with the reproduced material.

    Reproduced material should be attributed as follows:

    • For reproduction of material from NJC:
      [Original citation] - Published by The Royal Society of Chemistry (RSC) on behalf of the Centre National de la Recherche Scientifique (CNRS) and the RSC.
    • For reproduction of material from PCCP:
      [Original citation] - Published by the PCCP Owner Societies.
    • For reproduction of material from PPS:
      [Original citation] - Published by The Royal Society of Chemistry (RSC) on behalf of the European Society for Photobiology, the European Photochemistry Association, and RSC.
    • For reproduction of material from all other RSC journals:
      [Original citation] - Published by The Royal Society of Chemistry.

    Information about reproducing material from RSC articles with different licences is available on our Permission Requests page.

Search articles by author

Spotlight

Advertisements