Literature DB >> 12916059

Non-thiol farnesyltransferase inhibitors: FTase-inhibition and cellular activity of benzophenone-based bisubstrate analogue farnesyltransferase inhibitors.

Andreas Mitsch1, Silke Bergemann, Ronald Gust, Isabel Sattler, Martin Schlitzer.   

Abstract

Some 5-acylaminoacylamino-benzophenone derivatives were designed as bisubstrate analogue farnesyltransferase inhibitors. These compounds turned out to be only weakly active against farnesyltransferase, but displayed an antiproliferative effect rendering them suitable for further development as a novel type of cytostatic agents.

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Year:  2003        PMID: 12916059     DOI: 10.1002/ardp.200300758

Source DB:  PubMed          Journal:  Arch Pharm (Weinheim)        ISSN: 0365-6233            Impact factor:   3.751


  2 in total

Review 1.  Unraveling the mechanism of the farnesyltransferase enzyme.

Authors:  Sérgio Filipe Sousa; Pedro Alexandrino Fernandes; Maria João Ramos
Journal:  J Biol Inorg Chem       Date:  2004-12-21       Impact factor: 3.358

2.  Protein farnesyltransferase-catalyzed isoprenoid transfer to peptide depends on lipid size and shape, not hydrophobicity.

Authors:  Thangaiah Subramanian; Suxia Liu; Jerry M Troutman; Douglas A Andres; H Peter Spielmann
Journal:  Chembiochem       Date:  2008-11-24       Impact factor: 3.164

  2 in total

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