Results 301 to 310 of about 112,073 (318)
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Modulation of ribonuclease P activity by calcipotriol
European Journal of Biochemistry, 2000The effects of cholesterol, 7‐dehydrocholesterol, vitamin D3 and several synthetic vitamin D3 analogs on ribonuclease P (RNase P) were investigated using a cell‐free system from the slime mold Dictyostelium discoideum. RNase P is an ubiquitous and essential enzyme that endonucleolytically cleaves all tRNA precursors to produce the mature 5′ end.
E, Papadimou +4 more
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Structure of ribonuclease P — a universal ribozyme
Current Opinion in Structural Biology, 2006Ribonuclease P (RNase P) is one of only two known universal ribozymes and was one of the first ribozymes to be discovered. It is involved in RNA processing, in particular the 5' maturation of tRNA. Unlike most other natural ribozymes, it recognizes and cleaves its substrate in trans. RNase P is a ribonucleoprotein complex containing one RNA subunit and
Alfredo, Torres-Larios +3 more
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1988
Ribonuclease P is an enzyme that cleaves tRNA precursors to generate the 5’ termini of mature tRNA sequences. In E. coli this enzyme consists of a catalytic RNA subunit and a protein cofactor. In the absence of direct cloning of the gene for the RNA component and functional assays of the transcript of that cloned gene, it is possible to perform other ...
Sidney Altman +2 more
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Ribonuclease P is an enzyme that cleaves tRNA precursors to generate the 5’ termini of mature tRNA sequences. In E. coli this enzyme consists of a catalytic RNA subunit and a protein cofactor. In the absence of direct cloning of the gene for the RNA component and functional assays of the transcript of that cloned gene, it is possible to perform other ...
Sidney Altman +2 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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Modifications of ribonuclease A induced by p-benzoquinone
Bioorganic Chemistry, 2012The nature of ribonuclease A (RNase) modifications induced by p-benzoquinone (pBQ) was investigated using several analysis methods. SDS-PAGE experiments revealed that pBQ was efficient in producing oligomers and polymeric aggregates when RNase was incubated with pBQ.
Jisook, Kim +4 more
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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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2009
Two gene-targeting approaches have been developed with the use of RNase P. The first approach is based on an external guide sequence (EGS), which consists of a sequence complementary to a target mRNA and, when noncovalently complexed with RNase P, renders the target RNA susceptible to degradation by the ribonuclease.
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Two gene-targeting approaches have been developed with the use of RNase P. The first approach is based on an external guide sequence (EGS), which consists of a sequence complementary to a target mRNA and, when noncovalently complexed with RNase P, renders the target RNA susceptible to degradation by the ribonuclease.
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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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