eprintid: 22263
rev_number: 26
userid: 1419
dir: disk0/00/02/22/63
datestamp: 2014-07-18 21:00:58
lastmod: 2021-06-12 22:55:54
status_changed: 2014-07-18 21:00:58
type: article
metadata_visibility: show
item_issues_count: 0
eprint_status: archive
creators_name: Wipf, P
creators_name: Hopkins, CR
creators_name: Phillips, EO
creators_name: Lazo, JS
creators_email: pwipf@pitt.edu
creators_email: 
creators_email: 
creators_email: 
creators_id: PWIPF
creators_id: 
creators_id: 
creators_id: 
title: Separation of Cdc25 dual specificity phosphatase inhibition and DNA cleaving activities in a focused library of analogs of the antitumor antibiotic Dnacin
ispublished: pub
divisions: sch_as_chemistry
full_text_status: public
abstract: Biological evaluation of 96 analogs and synthetic intermediates of the naphthyridinomycin-type antitumor antibiotic Dnacin led to the identification of several low-micromolar inhibitors of dual specificity phosphatases, specifically Cdc25A1, Cdc25B2, and VHR, as well as the tyrosine phosphatase PTP1B. While the parent Dnacins are potent DNA cleavage agents, most of the analog structures, even those that retained significant phosphatase inhibitory activities, did not lead to plasmid DNA cleavage. Thus, the DNA-targeting and the phosphatase-inhibitory activities of Dnacins can be assigned to different pharmacophores. © 2002 Elsevier Science Ltd. All rights reserved.
date: 2002-08-05
date_type: published
publication: Tetrahedron
volume: 58
number: 32
pagerange: 6367 - 6372
refereed: TRUE
issn: 0040-4020
id_number: 10.1016/S0040-4020(02)00636-1
citation:   Wipf, P and Hopkins, CR and Phillips, EO and Lazo, JS  (2002) Separation of Cdc25 dual specificity phosphatase inhibition and DNA cleaving activities in a focused library of analogs of the antitumor antibiotic Dnacin.  Tetrahedron, 58 (32).  6367 - 6372.  ISSN 0040-4020     
document_url: http://d-scholarship-dev.library.pitt.edu/22263/1/licence.txt