ArticleChemistry & biology2009
Structural basis for binding and selectivity of antimalarial and anticancer ethylenediamine inhibitors to protein farnesyltransferase.
Article in Chemistry & biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 37 citations in OpenAlex.
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- Pharmacophore modeling and in silico toxicity assessment of potential anticancer agents from African medicinal plants.Drug design, development and therapy · 2016Article
- Rapid analysis of protein farnesyltransferase substrate specificity using peptide libraries and isoprenoid diphosphate analogues.ACS chemical biology · 2014Article
- Crystal structures of the fungal pathogen Aspergillus fumigatus protein farnesyltransferase complexed with substrates and inhibitors reveal features for antifungal drug design.Protein science : a publication of the Protein Society · 2014Article
- Virtual lead identification of farnesyltransferase inhibitors based on ligand and structure-based pharmacophore techniques.Pharmaceuticals (Basel, Switzerland) · 2013Article
- Prenyltransferase Inhibitors: Treating Human Ailments from Cancer to Parasitic Infections.MedChemComm · 2013Article
- IADE: a system for intelligent automatic design of bioisosteric analogs.Journal of computer-aided molecular design · 2012Article
- Exploring protein lipidation with chemical biology.Chemical reviews · 2011Review
- Structures of Cryptococcus neoformans protein farnesyltransferase reveal strategies for developing inhibitors that target fungal pathogens.The Journal of biological chemistry · 2011Article
- Structure-based design and synthesis of potent, ethylenediamine-based, mammalian farnesyltransferase inhibitors as anticancer agents.Journal of medicinal chemistry · 2010Article
Corrections and comments
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Authors and funding
11 authors at 4 institutions in 1 country.
Funding
Abstract
Protein farnesyltransferase (FTase) catalyzes an essential posttranslational lipid modification of more than 60 proteins involved in intracellular signal transduction networks. FTase inhibitors have emerged as a significant target for development of anticancer therapeutics and, more recently, for the treatment of parasitic diseases caused by protozoan pathogens, including malaria (Plasmodium falciparum). We present the X-ray crystallographic structures of complexes of mammalian FTase with five inhibitors based on an ethylenediamine scaffold, two of which exhibit over 1000-fold selective inhibition of P. falciparum FTase. These structures reveal the dominant determinants in both the inhibitor and enzyme that control binding and selectivity. Comparison to a homology model constructed for the P. falciparum FTase suggests opportunities for further improving selectivity of a new generation of antimalarial inhibitors.
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Registered trials
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