Issue 3, 2012
From the journal:

MedChemComm

Quantitative affinity-based chemical proteomics of TrkA inhibitors†

Victoria E. Albrow,‡a   Carla Fernandes,‡b   David M. Beal,a   Matthew D. Selby,a   Mireia Fernandez-Ocaña,b   Klaus C. Rumpelb  and  Lyn H. Jones*ac  

* Corresponding authors

a Chemical Biology Group, World Wide Medicinal Chemistry, Sandwich Laboratories, Pfizer, Ramsgate Road, Sandwich, Kent, UK

b Structural Biology and Biophysics, World Wide Medicinal Chemistry, Sandwich Laboratories, Pfizer, Ramsgate Road, Sandwich, Kent, UK

c Chemical Biology and Orphan & Genetics Diseases, World Wide Medicinal Chemistry, Pfizer, 200 Cambridge Park Drive, Cambridge, MA, USA
E-mail: lyn.jones@pfizer.com
Tel: +1 617 665 5631

Abstract

Quantitative chemical proteomics enabled affinity-isolation and enrichment of the tyrosine receptor kinase TrkA and protein isolation was competed by the inhibitors purvalanol B and staurosporine in a dose-related manner. These methods will advance occupancy biomarker development and our understanding of TrkA biochemistry in disease.

Graphical abstract: Quantitative affinity-based chemical proteomics of TrkA inhibitors

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Article information

DOI
https://doi.org/10.1039/C2MD00271J
Article type
Concise Article
Submitted
25 Oct 2011
Accepted
22 Nov 2011
First published
02 Dec 2011

Med. Chem. Commun., 2012,3, 322-325

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Quantitative affinity-based chemical proteomics of TrkA inhibitors

V. E. Albrow, C. Fernandes, D. M. Beal, M. D. Selby, M. Fernandez-Ocaña, K. C. Rumpel and L. H. Jones, Med. Chem. Commun., 2012, 3, 322 DOI: 10.1039/C2MD00271J

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