Document Detail

Modulation of cofilin phosphorylation by inhibition of the Lim family kinases.
MedLine Citation:
PMID:  22902653     Owner:  NLM     Status:  Publisher    
A series of aminothiazoles that are potent inhibitors of LIM kinases 1 and 2 is described. Appropriate choice of substituents led to molecules with good selectivity for either enzyme. An advanced member of the series was shown to effectively interfere with the phosphorylation of the LIM kinases substrate cofilin. Consistent with the important role of the LIM kinases in regulating cytoskeletal structure, treated cells displayed dramatically reduced F-actin content.
Liqi He; Steven P Seitz; George L Trainor; David Tortolani; Wayne Vaccaro; Michael Poss; Christine M Tarby; John S Tokarski; Becky Penhallow; Chen-Yi Hung; Ricardo Attar; Tai-An Lin
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2012-7-21
Journal Detail:
Title:  Bioorganic & medicinal chemistry letters     Volume:  -     ISSN:  1464-3405     ISO Abbreviation:  Bioorg. Med. Chem. Lett.     Publication Date:  2012 Jul 
Date Detail:
Created Date:  2012-8-20     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9107377     Medline TA:  Bioorg Med Chem Lett     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Copyright Information:
Published by Elsevier Ltd.
Oncology Chemistry, Bristol-Myers Squibb Research and Development, Princeton, NJ 08543-4000, USA.
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