relation: http://d-scholarship-dev.library.pitt.edu/22178/
title: Synthesis and biological activity of a focused library of mitogen-activated protein kinase phosphatase inhibitors
creator: Arnold, DM
creator: Foster, C
creator: Huryn, DM
creator: Lazo, JS
creator: Johnston, PA
creator: Wipf, P
description: Mitogen-activated protein kinase phosphatase 1 is a tyrosine phosphatase superfamily member that dephosphorylates and inactivates mitogen-activated protein kinase substrates, such as p38, c-Jun-N-terminal kinase, and extracellular signal-related kinase. These mitogen-activated protein kinase substrates regulate many cellular processes associated with human diseases. In spite of this potential as a molecular target for chemotherapy, however, pharmacologically tractable inhibitors of mitogen-activated protein kinase phosphatase-1 have yet to be developed. Based on the results from a high-throughput screen for small molecule inhibitors of mitogen-activated protein kinase phosphatase-1, we designed, synthesized, and evaluated a focused library in an effort to further understand the structural requirements for mitogen-activated protein kinase phosphatase-1 inhibitory activity. © 2007 The Authors.
date: 2007-01-01
type: Article
type: PeerReviewed
format: text/plain
language: en
rights: attached
identifier: http://d-scholarship-dev.library.pitt.edu/22178/1/licence.txt
identifier:   Arnold, DM and Foster, C and Huryn, DM and Lazo, JS and Johnston, PA and Wipf, P  (2007) Synthesis and biological activity of a focused library of mitogen-activated protein kinase phosphatase inhibitors.  Chemical Biology and Drug Design, 69 (1).  23 - 30.  ISSN 1747-0277     
relation: 10.1111/j.1747-0285.2007.00474.x