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Acid ribonuclease activity of hepatoma cells [PDF]
, 1962 Activities of intracellular RNase of the liver cytoplasm, normal liver cells exposed to 3'-Me-DAB and heaptoma cells, have been studied in correlation with the contents of RNA and DNA and morphologic changes of the cells with or without treating RNase ...
Hayashi, Kenji +2 more
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Modeling the Thermoproteaceae RNase P RNA [PDF]
RNA Biology, 2012 The RNA component of the RNase P complex is found throughout most branches of the tree of life and is principally responsible for removing the 5' leader sequence from pre-tRNA transcripts during tRNA maturation. RNase P RNA has a number of universal core features, however variations in sequence and structure found in homologs across the tree of life ...
Chan, Patricia P. +2 more
openaire +2 more sources
RNase P-Mediated Sequence-Specific Cleavage of RNA by Engineered External Guide Sequences
Biomolecules, 2015 The RNA cleavage activity of RNase P can be employed to decrease the levels of specific RNAs and to study their function or even to eradicate pathogens. Two different technologies have been developed to use RNase P as a tool for RNA knockdown.
Merel Derksen +2 more
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Histochemical studies of adenosine triphosphatase activity of liver cells exposed to ribonuclease [PDF]
, 1962 It has been revealed that ribonuclease (RNase) can penetrate into living cells and inhibits amino acid incorporation into proteins resulting in the suppression of protein synthesis and growth of living cells.
Hayashi, Kenji, Kimoto, Tetsuo
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CHIMIA, 2018 Ribonuclease P (RNase P) is a class of enzymes involved in the processing of precursor tRNAs to remove their 5'-leader sequences. Ribonuclease P enzymes are classified into two completely distinct classes, i.e.
Yuri Nozawa +3 more
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RNase P — a ‘Scarlet Pimpernel’ [PDF]
Molecular Microbiology, 1995 RNase P is responsible for the maturation of the 5′‐termini of tRNA molecules in all cells studied to date. This ribonucleoprotein has to recognize and identify its cleavage site on a large number of different precursors. This review covers what is currently known about the function of the catalytic subunit of Escherichia coli RNase P, M1 RNA, and the ...
openaire +2 more sources
The role of ribonucleases in regulating global mRNA levels in the model organism Thermus thermophilus HB8 [PDF]
, 2014 BACKGROUND: RNA metabolism, including RNA synthesis and RNA degradation, is one of the most conserved biological systems and has been intensively studied; however, the degradation network of ribonucleases (RNases) and RNA substrates is not fully ...
Akeo Shinkai +7 more
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RNase MRP and RNase P share a common substrate
Nucleic Acids Research, 1993 RNase MRP is a site-specific ribonucleoprotein endoribonuclease that processes RNA from the mammalian mitochondrial displacement loop containing region. RNase P is a site-specific ribonucleoprotein endoribonuclease that processes pre-tRNAs to generate their mature 5'-ends.
T, Potuschak, W, Rossmanith, R, Karwan
openaire +3 more sources
PLoS Genetics, 2014 The RNase P family is a diverse group of endonucleases responsible for the removal of 5' extensions from tRNA precursors. The diversity of enzyme forms finds its extremes in the eukaryal nucleus where RNA-based catalysis by complex ribonucleoproteins in ...
Christoph Weber +3 more
doaj +1 more source
Comparative Analysis of Ribonuclease P RNA of the Planctomycetes [PDF]
, 2004 The planctomycetes, order Planctomycetales, are a distinct phylum of domain Bacteria. Genes encoding the RNA portion of ribonuclease P (RNase P) of some planctomycete members were sequenced and compared with existing database planctomycete sequences ...
Altman +61 more
core +1 more source