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Folding of a universal ribozyme: the ribonuclease P RNA
Quarterly Reviews of Biophysics, 2007AbstractRibonuclease P is among the first ribozymes discovered, and is the only ubiquitously occurring ribozyme besides the ribosome. The bacterial RNase P RNA is catalytically active without its protein subunit and has been studied for over two decades as a model system for RNA catalysis, structure and folding. This review focuses on the thermodynamic,
Nathan J, Baird +4 more
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Crystal structure of the specificity domain of ribonuclease P
Nature, 2003RNase P is the only endonuclease responsible for processing the 5' end of transfer RNA by cleaving a precursor and leading to tRNA maturation. It contains an RNA component and a protein component and has been identified in all organisms. It was one of the first catalytic RNAs identified and the first that acts as a multiple-turnover enzyme in vivo ...
Andrey S, Krasilnikov +3 more
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Structures of eukaryotic ribonuclease P
Science, 2018Structural Biology Ribonuclease P (RNase P) is a ribozyme that processes transfer RNA (tRNA) precursors and is found in all three kingdoms of life. Now, Lan et al. report the structures of yeast RNase P (see the Perspective by Scott and Nagai).
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Ribonucleoprotein Ribonucleases P and MRP
2011Ribonucleoprotein Ribonuclease (RNase) P and RNase MRP consist of a large RNA component and an essential protein part. RNases P/MRP differ from all other known ribonucleases in that it is their RNA component, not protein that is responsible for the endonucleolytic cleavage of substrates.
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Structural Studies of Ribonuclease P
2009RNase P is a universal ribozyme involved in RNA processing, in particular the maturation of the 5′ end of tRNA. Unlike most naturally occurring ribozymes, it recognizes and cleaves its substrate in trans and is capable of multiple turnovers. RNase P is a ribonucleoprotein complex containing one RNA subunit and as few as one protein subunit.
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