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pubmed-article:9224568pubmed:abstractTextEfficient operation of cellular processes relies on the strict control that each cell exerts over its metabolic pathways. Some protein enzymes are subject to allosteric regulation, in which binding sites located apart from the enzyme's active site can specifically recognize effector molecules and alter the catalytic rate of the enzyme via conformational changes. Although RNA also performs chemical reactions, no ribozymes are known to operate as true allosteric enzymes in biological systems. It has recently been established that small-molecule receptors can readily be made of RNA, as demonstrated by the in vitro selection of various RNA aptamers that can specifically bind corresponding ligand molecules. We set out to examine whether the catalytic activity of an existing ribozyme could be brought under the control of an effector molecule by designing conjoined aptamer-ribozyme complexes.lld:pubmed
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pubmed-article:9224568pubmed:articleTitleRational design of allosteric ribozymes.lld:pubmed
pubmed-article:9224568pubmed:affiliationDepartment of Molecular, Cellular and Developmental Biology, Yale University, New Haven, Connecticut, 06520-8103, USA.lld:pubmed
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