Results 21 to 30 of about 455,663 (298)

Function and assembly of a chromatin-associated RNase P that is required for efficient transcription by RNA polymerase I. [PDF]

open access: yesPLoS ONE, 2008
Human RNase P has been initially described as a tRNA processing enzyme, consisting of H1 RNA and at least ten distinct protein subunits. Recent findings, however, indicate that this catalytic ribonucleoprotein is also required for transcription of small ...
Robert Reiner   +3 more
doaj   +1 more source

The evolution of RNase P [PDF]

open access: yesRNA, 2015
Article and publication date are at http://www.rnajournal.org/cgi/doi/10.1261/rna.050732.115. Freely available online through the RNA Open Access option.
Engelke, David R., Fierke, Carol A.
openaire   +2 more sources

A novel mechanism of RNase L inhibition: Theiler\u27s virus L* protein prevents 2-5A from binding to RNase L [PDF]

open access: yes, 2018
The OAS/RNase L pathway is one of the best-characterized effector pathways of the IFN antiviral response. It inhibits the replication of many viruses and ultimately promotes apoptosis of infected cells, contributing to the control of virus spread ...
Drappier, Melissa   +8 more
core   +4 more sources

A functional RNase P protein subunit of bacterial origin in some eukaryotes [PDF]

open access: yes, 2011
RNase P catalyzes 5′-maturation of tRNAs. While bacterial RNase P comprises an RNA catalyst and a protein cofactor, the eukaryotic (nuclear) variant contains an RNA and up to ten proteins, all unrelated to the bacterial protein.
Bernal Bayard, Pilar   +5 more
core   +1 more source

Inhibition of Murine Cytomegalovirus Infection in Animals by RNase P-Associated External Guide Sequences. [PDF]

open access: yes, 2017
External guide sequence (EGS) RNAs are associated with ribonuclease P (RNase P), a tRNA processing enzyme, and represent promising agents for gene-targeting applications as they can direct RNase-P-mediated cleavage of a target mRNA.
Li, Wei   +9 more
core   +2 more sources

Zebrafish RNase T2 genes and the evolution of secretory ribonucleases in animals

open access: yesBMC Evolutionary Biology, 2009
Background Members of the Ribonuclease (RNase) T2 family are common models for enzymological studies, and their evolution has been well characterized in plants.
Essner Jeffrey J   +5 more
doaj   +1 more source

RNase P Branches Out from RNP to Protein: Organelle-Triggered Diversification? [PDF]

open access: yes, 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
core   +3 more sources

Genetic diversity of human RNase 8

open access: yesBMC Genomics, 2012
Background Ribonuclease 8 is a member of the RNase A family of secretory ribonucleases; orthologs of this gene have been found only in primate genomes. RNase 8 is a divergent paralog of RNase 7, which is lysine-enriched, highly conserved, has prominent ...
Chan Calvin C   +4 more
doaj   +1 more source

P finder: genomic and metagenomic annotation of RNase P RNA gene (rnpB)

open access: yesBMC Genomics, 2020
Background The rnpB gene encodes for an essential catalytic RNA (RNase P). Like other essential RNAs, RNase P’s sequence is highly variable. However, unlike other essential RNAs (i.e.
J. Christopher Ellis
doaj   +1 more source

Insights into the structure and activity of prototype foamy virus RNase H

open access: yesRetrovirology, 2012
Background RNase H is an endonuclease that hydrolyzes the RNA strand in RNA/DNA hybrids. Retroviral reverse transcriptases harbor a C-terminal RNase H domain whose activity is essential for viral replication.
Leo Berit   +4 more
doaj   +1 more source

Home - About - Disclaimer - Privacy