Results 131 to 140 of about 5,190 (143)
Some of the next articles are maybe not open access.

Purification of cytosolic, latent endoribonuclease from porcine thyroid

Archives of Biochemistry and Biophysics, 1982
Abstract An alkaline endoribonuclease was purified 1800-fold from the cytosolic, latent ribonuclease fraction of porcine thyroids by gentle procedures specifically designed to exclude both heating and acidification steps. Polyacrylamide gel electrophoresis revealed a broad peak of enzyme activity that was coincident with the stained protein band.
E E, Button, R, Guggenheimer, F J, Kull
openaire   +2 more sources

The Cmr complex: an RNA-guided endoribonuclease

Biochemical Society Transactions, 2013
The CRISPR (clustered regularly interspaced short palindromic repeats)–Cas (CRISPR-associated) system protects prokaryotes from infection by viruses and other potential genome invaders. This system represents an inheritable and adaptable immune system that is mediated by large ribonucleoprotein complexes, the CRISPR–Cas effector complexes.
openaire   +2 more sources

Characterization of an Endoribonuclease in Rat-Liver Nucleoli

European Journal of Biochemistry, 1974
Synthetic RNAs, i.e. [3H]poly(U) and [14C]poly(A), and natural RNAs, i.e. 16-S and 23-S Escherichia coli ribosomal [14C]RNA and MS2 coliphage [3H]RNA, were incompletely hydrolyzed by a rat liver nucleolar enzyme as measured by solubilization of radioactivity following ethanol precipitation.
A, Boctor, A, Grossman, W, Szer
openaire   +2 more sources

Cleavage site recognition by the tRNA splicing endoribonuclease

Gene, 1993
A single tRNA-splicing endoribonuclease can cleave several precursors. In addition to the conserved nucleotides (nt), there are positions in the mature domain that, though not always occupied by the same nt, nevertheless play a fundamental role in intron excision reaction. The elements of the recognition set (invariant nt, nt at the cardinal positions)
G P, Tocchini-Valentini   +3 more
openaire   +2 more sources

[Synthetic endoribonucleases].

Molekuliarnaia biologiia, 1993
The data on the synthesis of RNA-fragments with endoribonuclease activity were reviewed. In the framework of the hammerhead model refined by Haselof and Gerlach the contribution of certain nucleotides or functional groups in ribozyme catalytic activity and the role of double helices are considered in detail.
openaire   +1 more source

Endoribonuclease IV. 2. Further Investigation on the Specificity

European Journal of Biochemistry, 1976
The poly(A)-specific endoribonuclease IV produces oligo(A) fragments of a chain length of 10 AMP nucleotides. One enzyme molecule performs 1700 cleavages per min; the cleavages occur randomly. The endoribonuclease IV is a nuclear enzyme which is present in the oviduct of quails in a concentration of 40 000 enzyme molecules per cell. Poly(A) segments on
W E, Müller   +3 more
openaire   +2 more sources

Staphylococcus aureus endoribonuclease III purification and properties.

Methods in enzymology, 2008
Staphylococcus aureus ribonuclease III (Sa-RNase III) belongs to the enzyme family known to process double-stranded RNAs consisting of two turns of the RNA helix. Although the enzyme is thought to play a role in ribosomal RNA processing and gene regulation, the deletion of the rnc gene in S. aureus does not affect cell growth in rich medium. S.
Chevalier, C.   +6 more
openaire   +2 more sources

Recombinant proteasome alpha-type subunits exhibit endoribonuclease activity

Cell and Tissue Biology, 2011
26S proteasome is a multi-subunit protein complex that consists of the regulatory 19S and the catalytic 20S subcomplexes. The major cellular function of the proteasome is protein degradation. It has been found recently that the 20S particle, besides its proteolytic activity, also possesses endoribonuclease activity.
O A, Fedorova   +3 more
openaire   +2 more sources

RNA Recognition and Cleavage by Sequence-Specific Endoribonucleases

Protein & Peptide Letters, 2007
Inactivation of RNA molecules by sequence-specific endoribonucleolytic cleavage is a subtle mechanism by which cells regulate gene expression. Sequence-specific endoribonucleases can recognize and cleave particular phosphodiester bonds confined within hundreds/thousands of chemically similar bonds.
Fakhri, Saïda, Benoît, Odaert
openaire   +2 more sources

Home - About - Disclaimer - Privacy