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- W2087281292 abstract "Ribosome-inactivating proteins (RIPs) are a group of proteins that inhibit protein synthesis in eucaryotic cells. While the biological effects have been well characterized, the underlying enzymatic mechanisms have not been elucidated until recently. Two different mechanisms have been identified. Plant and bacterial RIPs act as N-glycosidases. They cleave a single N-glycosidic bond between adenine and ribose at a specific nucleotide A-4324 of the 28S rRNA of the 60S ribosomal subunit. On the other hand, the fungal RIPs act as ribonucleases and cleave a single phosphodiester bond between G-4325 and A-4326 of the same rRNA, just one nucleotide away from the site of action of plant/bacterial RIPs. Other protein synthesis inhibitory proteins act by their ADP-ribosyltransferase activity which modify and thus inactivate elongation factor-2. Recently, some toxins have been shown to possess deoxyribonuclease activity which may also account for their toxicity." @default.
- W2087281292 created "2016-06-24" @default.
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- W2087281292 creator A5080196361 @default.
- W2087281292 date "1991-01-01" @default.
- W2087281292 modified "2023-09-25" @default.
- W2087281292 title "Enzymatic properties of ribosome-inactivating proteins (RIPs) and related toxins" @default.
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- W2087281292 doi "https://doi.org/10.1016/0024-3205(91)90286-k" @default.
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