Carrot and stick: how RNase R contributes to function and destruction of the translation machinery. [PDF]
Paternoga H, Dimitrova-Paternoga L.
europepmc +1 more source
Loop-mediated regulation and base flipping drive RNA cleavage by human mitochondrial PNPase. [PDF]
Unseld O, Das H, Hällberg BM.
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Targeting interferon-stimulated gene of 20 kDa protein (Isg20) inhibits ribosome biogenesis to ameliorate the progression of renal fibrosis. [PDF]
Liu X, Wang H, Wang K, Liu Y.
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The Impact of Chemical Modifications on the Interferon-Inducing and Antiproliferative Activity of Short Double-Stranded Immunostimulating RNA. [PDF]
Bishani A +3 more
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RNA 3'end tailing safeguards cells against products of pervasive transcription termination. [PDF]
Wu G +3 more
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Drosophila 5′ → 3′-Exoribonuclease Pacman
Methods in enzymology, 2001Publisher Summary This chapter concentrates on the methods used to express a Drosophila recombinat 5′ → 3′-exoribonuclease, purify the protein, and analyze its activity in vitro . Analysis of early development in Drosophila has shown that RNA localization, control of translation, and mRNA stability are intimately linked.
I V, Chernukhin +2 more
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Exoribonucleases and Endoribonucleases
EcoSal Plus, 2004This review provides a description of the known Escherichia coli ribonucleases (RNases), focusing on their structures, catalytic properties, genes, physiological roles, and possible regulation. Currently, eight E. coli exoribonucleases are known.
Zhongwei, Li, Murray P, Deutscher
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Escherichiacoli mutants deficient in exoribonucleases
Biochemical and Biophysical Research Communications, 1976Abstract Strain S296, isolated by screening 2000 colonies after nitrosoguanidine mutagenesis, yields extracts with less than 1% of wild-type RNase activity against ( 3 H) poly(U). Unlike other E. coli strains, S296 grows with a doubling time of about 2 hr., both in nutrient broth and in minimal medium, and at 30°, 37° and 42°. The strain retains
N, Nikolaev, V, Folsom, D, Schlessinger
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A microsomal exoribonuclease from rat liver
Biochimica et Biophysica Acta (BBA) - Enzymology, 1979A exoribonuclease has been purified from the microsomes of rat liver. The enzyme had an apparent molecular weight of 80 000-83 000 and produced, via a processive mechanism, 5'-AMP as the only product from poly(A). The degradation was found to proceed in the 3' to 5' direction.
H, Kumagai +4 more
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Structures of 5′–3′ Exoribonucleases
20125'-3' Exoribonucleases (XRNs) have important functions in RNA processing, RNA turnover and decay, RNA interference, RNA polymerase transcription, and other cellular processes. Their sequences share two highly conserved regions, CR1 and CR2. The cytoplasmic Xrn1 and the nuclear Xrn2/Rat1 are found in yeast and animals, and XRNs are found in most other ...
Jeong Ho, Chang +2 more
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