Results 31 to 40 of about 436,820 (281)
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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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 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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Human RNase H1 is associated with protein P32 and is involved in mitochondrial pre-rRNA processing. [PDF]
PLoS ONE, 2013 Mammalian RNase H1 has been implicated in mitochondrial DNA replication and RNA processing and is required for embryonic development. We identified the mitochondrial protein P32 that binds specifically to human RNase H1, but not human RNase H2. P32 binds
Hongjiang Wu +4 more
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Protein synthesis inhibitors and catalytic RNA Effect of puromycin on tRNA precursor processing by the RNA component of Escherichia coli RNase P [PDF]
, 1989 RNase P and ribosomes must interact with similar substrate molecules, tRNA precursors in the case of RNase P and aminoacyl-, peptidyl- or free tRNAs in the case of ribosomes.
Direcció Tècnica d'Urbanisme +1 more
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Cell Reports, 2012 RNase P is the endonuclease that removes 5′ extensions from tRNA precursors. In its best-known form, the enzyme is composed of a catalytic RNA and a protein moiety variable in number and mass. This ribonucleoprotein enzyme is widely considered ubiquitous
Andreas Taschner +5 more
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A Novel Method to Isolate RNase MRP Using RNA Streptavidin Aptamer Tags
Bio-Protocol, 2023 Interactions between RNA-binding proteins and RNA molecules are at the center of multiple biological processes. Therefore, accurate characterization of the composition of ribonucleoprotein complexes (RNPs) is crucial.
Violette Charteau +2 more
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RNA synthesis in mitochondria isolated from rat liver [PDF]
, 1977 Mitochondrial RNA (mtRNA) was synthesized from purine and pyrimidine nucleosides in coupling with oxidative phosphorylation using isolated mitochondria. The in vivo synthesized mtRNA was adenine-uracil rich and sedimented at about 20 S by sucrose density
Inaba, Kozo, Oda, Takuzo
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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
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