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Wireless Bioelectronic Modulation of Membrane Potential in Glioblastoma Using Carbon Nanotube Porins

open access: yesAdvanced Science, EarlyView.
A schematic illustrating glioblastoma cell membrane modulation using carbon nanotube porins (CNTPs) and an applied voltage. CNTPs enable ion flux leading to changes in membrane potential. This figure summarizes the concept of bioelectronic control of cell membrane voltage.
Fleur Groualle   +6 more
wiley   +1 more source
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Life without RNase P

Nature, 2008
The universality of ribonuclease P (RNase P), the ribonucleoprotein essential for transfer RNA (tRNA) 5' maturation, is challenged in the archaeon Nanoarchaeum equitans. Neither extensive computational analysis of the genome nor biochemical tests in cell extracts revealed the existence of this enzyme.
Lennart, Randau   +2 more
openaire   +2 more sources

Plant mitochondrial RNase P

Molecular Biology Reports, 1996
Molecular investigations in mitochondria of higher plants have to take in account the complicated genomic structure of these organelles and their complex mode of gene expression. Recently tRNA processing activities and particularly RNase P-like activities have been described for mitochondria of mono- and dicot plants.
openaire   +2 more sources

RNase P RNA ofMycoplasma capricolum

Molecular Biology Reports, 1996
There are at least six small stable RNAs in Mycoplasma capricolum cells besides tRNAs and rRNAs. One of them, MCS5 RNA, is a homolog of RNase P RNA. The predicted secondary structure of this RNA is essentially the same as that of other eubacterial RNase P RNAs. MCS5 RNA is more similar to the RNase P RNA of B. Subtilis than to that of E. coli.
C, Ushida, D, Izawa, A, Muto
openaire   +2 more sources

Eukaryote RNase P and RNase MRP

2009
Ribonuclease P (RNase P) is an essential endonuclease that catalyzes the cleavage of the 5′ leader sequence from precursor tRNAs (pre-tRNAs). Most forms of RNase P are ribonucleoproteins and the bacterial enzyme possesses a single catalytic RNA and one small protein.
Scott C. Walker   +2 more
openaire   +1 more source

A novel protein shared by RNase MRP and RNase P

RNA (New York, N.Y.), 1997
We have isolated suppressors of the temperature-sensitive rRNA processing mutation rrp2-2 in Saccharomyces cerevisiae. A class of extragenic suppressors was mapped to the YBR257w reading frame in the right arm of Chromosome II. Characterization of this gene, renamed POP4, shows that the gene product is necessary both for normal 5.8S rRNA processing and
S, Chu, J M, Zengel, L, Lindahl
openaire   +2 more sources

RNase P RNA-mediated catalysis

Biochemical Society Transactions, 2002
The endoribonuclease RNase P is involved in the processing of tRNA precursors to generate mature 5′ termini. The catalytic activity of RNase P is associated with an RNA, RNase P RNA. A specific interaction between the 3′ end of the substrate and RNase P RNA, to form an RNase P RNA-substrate complex, is referred to as the ‘73–294-interaction’.
openaire   +2 more sources

Structural Studies of RNase P

Annual Review of Biophysics, 2013
Ribonuclease P (RNase P) is one of the first ribozymes discovered and it is found in all phylogenetic groups. It is responsible for processing the 5′ end of pre-tRNAs as well as other RNA molecules. RNase P is formed by an RNA molecule responsible for catalysis and one or more proteins.
openaire   +2 more sources

A view of RNase P

Molecular BioSystems, 2007
Major progress in the study of RNase P has resulted from crystallography of bacterial catalytic subunits and the discovery of catalytic activity in eukaryotes. Several new substrates have also been identified, primarily in bacteria but also in yeast. Our current world should be called the "RNA-protein world" rather than the "protein world".
openaire   +2 more sources

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