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• W2022892730 abstract "Lipid modification of eukaryotic proteins by protein prenyltransferases is required for critical signaling pathways, cell cycle progression, cytoskeleton remodeling, induction of apoptosis and vesicular trafficking. This review analyzes the influence of distinct states of sequential posttranslational processing that can be obtained after single or double prenylation, reversible palmitoylation, proteolytic cleavage of the C-terminus and possible reversible carboxymethylation. This series of modifications, as well as the exact length of the prenyl anchor, are determinants in protein-membrane and specific protein-protein interactions of protein prenyltransferase substrates. Furthermore, the occurrence and distribution of pseudogenes of protein prenyltransferase subunits are discussed. Besides being developed as anti-cancer agents, prenyltransferase inhibitors are effective against an increasing number of parasitic diseases. Extensive screens for protein prenyltransferases in genomic data of fungal and protozoan pathogens unveil a series of new pharmacologic targets for prenyltransferase inhibition, including the parasites Brugia malayi, Onchocerca volvulus, Aspergillus nidulans, Pneumocystis carinii, Entamoeba histolytica, Strongyloides stercoralis, Trichinella spiralis and Cryptosporidium parvum." @default.
• W2022892730 created "2016-06-24" @default.
• W2022892730 creator A5007579711 @default.
• W2022892730 creator A5019975803 @default.
• W2022892730 creator A5041330491 @default.
• W2022892730 date "2003-01-15" @default.
• W2022892730 modified "2023-10-18" @default.
• W2022892730 title "Protein Prenyltransferases: Anchor Size, Pseudogenes and Parasites" @default.
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• W2022892730 doi "https://doi.org/10.1515/bc.2003.110" @default.
• W2022892730 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/12956414" @default.
• W2022892730 hasPublicationYear "2003" @default.
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