Results 271 to 280 of about 1,979,759 (307)

Distinguishing self from non-self RNA by editing-specific inosine patterns

Varada R, Leuchtenberger A, Vesely C, Kaczmarek B, Khosravi HM, Mandl T, Milanovic K, Tamizkar KH, Rajendra V, Senoner H, Steinbichl L, Borojevic M, Sombke A, Schmidt K, Eckhard M, Hofacker I, Walkley C, Heraud-Farlow J, Picardi E, Bernecky C, Jantsch M.   +20 more
europepmc   +1 more source

pH-Reversible Cationic RNase A Conjugates for Enhanced Cellular Delivery and Tumor Cell Killing

Biomacromolecules, 2015
Intracellularly-acting therapeutic proteins are considered promising alternatives for the treatment of various diseases. Major limitations of their application are low efficiency of intracellular delivery and possible reduction of protein activity during
Xiaowen Liu, Peng Zhang, Dongsheng He, Wolfgang Rödl, Tobias Preiß, Joachim O. Rädler, Ernst Wagner, Ulrich Lächelt   +7 more
semanticscholar   +4 more sources

RNase PH catalyzes a synthetic reaction, the addition of nucleotides to the 3′ end of RNA

Biochimie, 1990
Escherichia coli RNase PH is a phosphate-dependent exoribonuclease that has been implicated in the 3' processing of tRNA precursors. It degrades RNA chains in a phosphorolytic manner releasing nucleoside diphosphates as products. Here we show that RNase PH also catalyzes a synthetic reaction, the addition of nucleotides to the 3' termini of RNA ...
K A Ost, Murray P. Deutscher
semanticscholar   +5 more sources

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Structure of the Methanothermobacter thermautotrophicus exosome RNase PH ring.

Acta Crystallographica Section D Biological Crystallography, 2010
The core of the exosome, a versatile multisubunit RNA-processing enzyme found in archaea and eukaryotes, includes a ring of six RNase PH subunits. This basic architecture is homologous to those of the bacterial and archaeal RNase PHs and the bacterial ...
C. Ng, D. Waterman, A. Antson, M. Ortíz-Lombardía   +3 more
semanticscholar   +4 more sources

The TCL1 oncoprotein binds the RNase PH domains of the PNPase exoribonuclease without affecting its RNA degrading activity

Cancer Letters, 2006
TCL1 is an AKT kinase coactivator that, when dysregulated, initiates mature lymphocyte malignancies in humans and transgenic mice. While TCL1 augments AKT pathway signaling, additional TCL1 interacting proteins that may contribute to cellular homeostasis or transformation are lacking.
Samuel W. French, David W. Dawson, Hsiao‐Wen Chen, Robert N. Rainey, Stuart A. Sievers, Cynthia E. Balatoni, Larry Wong, Joshua J. Troke, Mai Nguyen, Carla M. Koehler, Michael A. Teitell   +10 more
semanticscholar   +5 more sources

Equilibrium unfolding of RNase Rs from Rhizopus stolonifer: pH dependence of chemical and thermal denaturation

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2003
The conformational stability of RNase Rs was determined with chemical and thermal denaturants over the pH range of 1-10. Equilibrium unfolding with urea showed that values of D(1/2) (5.7 M) and DeltaG(H(2)O) (12.8 kcal/mol) were highest at pH 5.0, its pI and the maximum conformational stability of RNase Rs was observed near pH 5.0.
Rajashree A. Deshpande, M. Islam Khan, Vepatu Shankar   +2 more
semanticscholar   +5 more sources

The pH-dependence of the Escherichia coli RNase HII-catalysed Reaction Suggests that an Active Site Carboxylate Group Participates Directly in Catalysis

Journal of Molecular Biology, 2007
RNase HII specifically catalyses the hydrolysis of phosphate diester linkages contained within the RNA portion of DNA/RNA hybrids. The catalytic parameters of the enzyme derived from Escherichia coli BL21 have been measured using 5'-fluorescent oligodeoxynucleotide substrates containing embedded ribonucleotides.
James A. Bastock, Michelle Webb, Jane A. Grasby   +2 more
semanticscholar   +6 more sources

pH profile of kinetic constants of RNase Rh from Rhizopus niveus and its mutant enzymes towards UpU, and possible mechanisms of RNase Rh.

The Journal of Biochemistry, 1994
In order to elucidate the mechanism of action of Rhizopus niveus RNase Rh, we investigated the pH profiles of the kinetic parameters of RNase RNAP Rh, a derivative of RNase Rh, and its mutant enzymes, i.e., RNase RNAP Rh H104F, RNase RNAP Rh E105Q, and ...
M. Irie, K. Ohgi, H. Watanabe, M. Iwama, K. Nakamura, H. Kurihara, T. Nonaka, Y. Mitsui, H. Horiuchi, M. Takagi   +9 more
semanticscholar   +4 more sources

Cleavage site selection by M1 RNA the catalytic subunit of Escherichia coli RNase P, is influenced by pH.

Journal of Molecular Biology, 1994
We have studied cleavage site selection by M1 RNA, the catalytic subunit of Escherichia coli RNase P, under various reaction conditions using tRNA precursors which are cleaved at two positions.
J. Kufel, L. Kirsebom
semanticscholar   +3 more sources

Equilibrium unfolding of A. niger RNase: pH dependence of chemical and thermal denaturation

European Biophysics Journal, 2011
Equilibrium unfolding of A. niger RNase with chemical denaturants, for example GuHCl and urea, and thermal unfolding have been studied as a function of pH using fluorescence, far-UV, near-UV, and absorbance spectroscopy. Because of their ability to affect electrostatic interactions, pH and chemical denaturants have a marked effect on the stability ...
G. R. Kumar, Anurag Sharma, Moni Kumari, M. Jagannadham, M. Debnath   +4 more
semanticscholar   +4 more sources