Recently, the possibility of developing drugs that knock out the unwanted
genetic function associated with unique RNA structures has led laboratories
in industry and academia to screen for medicinal compounds directed
to disease-associated RNA targets.
Small molecules that influence RNA directed activity are to be screened from large combinatorial libraries of compounds. To date, most accumulated knowledge in this field centers around the development of drugs that offer therapies against infectious diseases. For example, drug discovery related to hepatitis C virus infection targets a unique translation control signal, the internal ribosome initiation site (IRES), which is essential for the viral life cycle (Anwar, Ali, Tanveer, & Siddiqui, 2000).
We will discuss the RNA structure formed by the 5' untranslated region (5'UTR) of the endogenous amyloid precursor protein (APP) gene (APP 5'UTR) as a therapeutic drug target for Alzheimer's disease (AD) (Figure 11.1) (Rogers et al., 1999). Interleukin-1 and iron regulate APP gene expression at the translational level through the APP 5'UTR, similar to the iron-storage protein, ferritin (Rogers, 1996, 1999). This finding is consistent with the fact that the secreted ectodomain of the precursor (APPs) binds (and probably sequesters) the neurotoxic metals, copper, and iron.
Small molecules that influence RNA directed activity are to be screened from large combinatorial libraries of compounds. To date, most accumulated knowledge in this field centers around the development of drugs that offer therapies against infectious diseases. For example, drug discovery related to hepatitis C virus infection targets a unique translation control signal, the internal ribosome initiation site (IRES), which is essential for the viral life cycle (Anwar, Ali, Tanveer, & Siddiqui, 2000).
We will discuss the RNA structure formed by the 5' untranslated region (5'UTR) of the endogenous amyloid precursor protein (APP) gene (APP 5'UTR) as a therapeutic drug target for Alzheimer's disease (AD) (Figure 11.1) (Rogers et al., 1999). Interleukin-1 and iron regulate APP gene expression at the translational level through the APP 5'UTR, similar to the iron-storage protein, ferritin (Rogers, 1996, 1999). This finding is consistent with the fact that the secreted ectodomain of the precursor (APPs) binds (and probably sequesters) the neurotoxic metals, copper, and iron.
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