|1.||Barbas, Ana: 2 articles (06/2011 - 09/2006)|
|2.||Awano, Naoki: 2 articles (03/2010 - 09/2008)|
|3.||Phadtare, Sangita: 2 articles (03/2010 - 09/2008)|
|4.||Inouye, Masayori: 2 articles (03/2010 - 09/2008)|
|5.||Krasich, Rachel: 1 article (04/2015)|
|6.||Kuo, H Kenny: 1 article (04/2015)|
|7.||Kreuzer, Kenneth N: 1 article (04/2015)|
|8.||Wu, Sunny Yang: 1 article (04/2015)|
|9.||Gómez-Puertas, Paulino: 1 article (06/2011)|
|10.||Matos, Rute Gonçalves: 1 article (06/2011)|
06/01/1974 - "In strain N464 at the non-permissive temperature the ribonuclease II activity may be decreased by 50% without effect upon the amount of p16S rRNA, whereas in methionine starvation of this strain the enzyme activity is at a maximum and the p16S rRNA is eight times that in exponential-phase cells. "
12/01/1971 - "Extracts of this mutant strain show an increased ribonuclease II activity as compared to extracts of the parental strain, and stable ribonucleic acid is degraded to a larger extent in this strain during starvation. "
02/01/2011 - "During starvation, the exoribonucleases RNase II and RNase R are important for fragment removal, whereas for quality control, RNase R and PNPase are more important. "
01/10/1974 - "The involvement of ribonuclease I, ribonuclease II, and polynucleotide phosphorylase in the degradation of stable ribonucleic acid during carbon starvation in Escherichia coli."
06/01/2011 - "RNase II and RNase R share structural properties, including 60% of amino acid sequence similarity and have a similar modular domain organization: two N-terminal cold shock domains (CSD1 and CSD2), one central RNB catalytic domain, and one C-terminal S1 domain. "
09/07/2006 - "Here we report the X-ray crystallographic structures of both the ligand-free (at 2.44 A resolution) and RNA-bound (at 2.74 A resolution) forms of Escherichia coli RNase II. In contrast to sequence predictions, the structures show that RNase II is organized into four domains: two cold-shock domains, one RNB catalytic domain, which has an unprecedented alphabeta-fold, and one S1 domain. "
03/01/2010 - "coli, such as polynucleotide phosphorylase and RNase II, cannot complement the cold shock function of CsdA. "
09/01/2008 - "coli genomic library for an in vivo counterpart of PNPase that can compensate for its absence at low temperature revealed only one protein, another 3'-to-5' exonuclease, RNase II. Here we show that the RNase PH domains 1 and 2 of PNPase are important for its cold shock function, suggesting that the RNase activity of PNPase is critical for its essential function at low temperature. "
10/01/2005 - "Mutants defective in ribonuclease II and polynucleotide phosphorylase demonstrated hypersensitivity to the antibiotic and showed a greater extent of 23S rRNA accumulation and a slower recovery rate. "
04/01/2015 - "Mutational inactivation of functions involved in mRNA processing and RNA polymerase elongation/release (RNase II, RNaseD, RNase PH, RNase LS, Rep, HepA, GreA, GreB) did not cause aza-C hypersensitivity; the mechanism of tmRNA access remains unclear. "
|1.||RNA (Ribonucleic Acid)
|3.||Polyribonucleotide Nucleotidyltransferase (Polynucleotide Phosphorylase)
|4.||ribonuclease R (RNase R)
|5.||ribonuclease PH (RNase PH)
|6.||Messenger RNA (mRNA)
|7.||DNA-Directed RNA Polymerases (RNA Polymerase)
|8.||Pancreatic Ribonuclease (Ribonuclease A)