Results 51 to 60 of about 430,076 (284)
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
core +1 more source
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
doaj +1 more source
Chance and necessity in the evolution of RNase P [PDF]
RNA, 2017 RNase P catalyzes 5′-maturation of tRNAs in all three domains of life. This primary function is accomplished by either a ribozyme-centered ribonucleoprotein (RNP) or a protein-only variant (with one to three polypeptides). The large, multicomponent archaeal and eukaryotic RNase P RNPs appear disproportionate to the simplicity of their role in tRNA 5 ...
Andrey S. Krasilnikov +2 more
openaire +2 more sources
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
core +1 more source
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
Unexpected diversity of RNase P, an ancient tRNA processing enzyme: challenges and prospects [PDF]
, 2010 For an enzyme functioning predominantly in a seemingly housekeeping role of 5′ tRNA maturation, RNase P displays a remarkable diversity in subunit make-up across the three domains of life.
Gopalan, Venkat +3 more
core +1 more source
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
doaj +1 more source
hPop5, a Protein Subunit of the Human RNase MRP and RNase P Endoribonucleases [PDF]
Journal of Biological Chemistry, 2001 The RNase MRP and RNase P particles both function as endoribonucleases. RNase MRP has been implicated in the processing of precursor-rRNA, whereas RNase P has been shown to function in the processing of pre-tRNA. Both ribonucleoprotein particles have an RNA component that can be folded into a similar secondary structure and share several protein ...
Eenennaam, H. van +4 more
openaire +4 more sources
RNase P Ribozymes Inhibit the Replication of Human Cytomegalovirus by Targeting Essential Viral Capsid Proteins. [PDF]
, 2015 An engineered RNase P-based ribozyme variant, which was generated using the in vitro selection procedure, was used to target the overlapping mRNA region of two proteins essential for human cytomegalovirus (HCMV) replication: capsid assembly protein (AP ...
LIU, Fenyong +9 more
core +3 more sources
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
doaj +1 more source