Results 281 to 290 of about 112,073 (318)

CARF-dependent preferential RNA cleavage by Csm6 increases drug susceptibility of mycobacteria. [PDF]

open access: yesNucleic Acids Res
Wei W   +9 more
europepmc   +1 more source

RNase P generated tRF<sup>Ser-GCT</sup> promotes fat storage in adipocytes via Adrb2 signaling. [PDF]

open access: yesJ Biol Chem
Shen L   +14 more
europepmc   +1 more source
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Human Ribonuclease P

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
openaire   +2 more sources

The varieties of ribonuclease P

Trends in Biochemical Sciences, 1992
Ribonuclease 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
openaire   +2 more sources

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