Results 281 to 290 of about 112,073 (318)
CARF-dependent preferential RNA cleavage by Csm6 increases drug susceptibility of mycobacteria. [PDF]
Wei W +9 more
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Preliminary exploration of the relationship between ginsenoside content and endogenous hormones of multi stem ginseng and soil properties based on correlation analysis. [PDF]
Chen Y +5 more
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The structure and allelic diversity of the self-incompatibility locus (S-locus) in diploid potatoes inferred from genome sequences and transcriptome data from styles and pollen. [PDF]
Ames M, Halterman D, Bethke PC.
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RNase P generated tRF<sup>Ser-GCT</sup> promotes fat storage in adipocytes via Adrb2 signaling. [PDF]
Shen L +14 more
europepmc +1 more source
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2001
Publisher Summary Ribonuclease P is a ribonucleoprotein nuclease required for the site-specific cleavage of the 5′ leader sequence of precursor tRNAs. In eubacteria, the RNA subunit of RNase P is the catalytic moiety and is capable of processing precursor tRNA in the presence of divalent metal ions.
N, Jarrous, S, Altman
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Publisher Summary Ribonuclease P is a ribonucleoprotein nuclease required for the site-specific cleavage of the 5′ leader sequence of precursor tRNAs. In eubacteria, the RNA subunit of RNase P is the catalytic moiety and is capable of processing precursor tRNA in the presence of divalent metal ions.
N, Jarrous, S, Altman
openaire +2 more sources
The varieties of ribonuclease P
Trends in Biochemical Sciences, 1992Ribonuclease P is a ribozyme involved in tRNA processing that is present in all cells and organelles that synthesize tRNA. Most of our understanding of ribonuclease P derives from studies of the bacterial enzyme. This enzyme has been characterized biochemically and a secondary structure for the RNA subunit has been proposed.
S C, Darr, J W, Brown, N R, Pace
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