Results 41 to 50 of about 508,134 (310)
Nature Communications, 2023 Ribonucleases (RNases) are responsible for RNA metabolism. RNase J, the core enzyme of the RNA degradosome, plays an essential role in global mRNA decay.
Luyao Bao +15 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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First biochemical characterization of a novel ribonuclease from wild mushroom Amanita hemibapha [PDF]
, 2012 A 45-kDa ribonuclease (RNase) was purified from dried fruiting bodies of the wild mushroom Amanita hemibapha. It was adsorbed on DEAE-cellulose, S-sepharose, and finally purified on Superdex 75. The RNase exhibited maximal RNase activity at pH 5 and in a
Bo Wang +4 more
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RUDN Journal of Ecology and Life SafetyThe activity of the complex of acid deoxyribonucleases (DNases) and ribonucleases (RNases) of the hepatopancreas of the river snail ( Viviparus viviparus L.) was studied under normal conditions and under acute exposure to erythromycin. An increase in the
Ekaterina A. Tishina +3 more
doaj +1 more source
Biologia Plantarum, 2018 In plants, class III T2 RNases involves two groups of structurally similar proteins, but with different biological functions: S-RNases and non-S-RNases.
H. J. Rojas +4 more
doaj +1 more source
The first crystal structure of human RNase6 reveals a novel substrate binding and cleavage site arrangement [PDF]
, 2016 Human RNase 6 is a cationic secreted protein that belongs to the RNase A superfamily. Its expression is induced in neutrophils and monocytes upon bacterial infection, suggesting a role in host defence.
Arranz Trullén, Javier +6 more
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Sequence determinants of RNA G‐quadruplex unfolding by Arg‐rich regions
FEBS Letters, EarlyView.We show that Arg‐rich peptides selectively unfold RNA G‐quadruplexes, but not RNA stem‐loops or DNA/RNA duplexes. This length‐dependent activity is inhibited by acidic residues and is conserved among SR and SR‐related proteins (SRSF1, SRSF3, SRSF9, U1‐70K, and U2AF1).
Naiduwadura Ivon Upekala De Silva +10 more
wiley +1 more source
RNase P Branches Out from RNP to Protein: Organelle-Triggered Diversification? [PDF]
, 2012 RNase P is the enzyme that removes 5′ leader sequences from precursor tRNAs. Remarkably, in most organisms, RNase P is a ribonucleoprotein particle where the RNA component is responsible for catalysis. In this issue of Genes \u26 Development, Gutmann and
Borah, Sumit +2 more
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Cell surface interactome analysis identifies TSPAN4 as a negative regulator of PD‐L1 in melanoma
Molecular Oncology, EarlyView.Using cell surface proximity biotinylation, we identified tetraspanin TSPAN4 within the PD‐L1 interactome of melanoma cells. TSPAN4 negatively regulates PD‐L1 expression and lateral mobility by limiting its interaction with CMTM6 and promoting PD‐L1 degradation.
Guus A. Franken +7 more
wiley +1 more source
Difference between Mitochondrial RNase P and Nuclear RNase P [Letters to the Editor] [PDF]
, 2001 [Discussion of: Puranam, R. S., and G. Attardi. 2001. The RNase P associated with HeLa cell mitochondria contains an essential RNA component identical in sequence to that of the nuclear RNase P. Mol. Cell. Biol. 21:548-561.
Attardi, Giuseppe +3 more
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