Results 261 to 270 of about 430,076 (284)
Early endonuclease-mediated evasion of RNA sensing ensures efficient coronavirus replication [PDF]
, 2017 Cervantes-Barragan, Luisa, et al.,
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Isolation and Molecular Evolution of the Selenocysteine tRNA (Cf TRSP) and RNase P RNA (Cf RPPH1) Genes in the Dog Family, Canidae [PDF]
, 2004 Carolyne Bardeleben +2 more
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Definition of the Th/ To ribonucleoprotein by RNase P and RNase MRP [PDF]
Molecular Biology Reports, 1993 We show that the Th/To ribonucleoprotein is defined by (i) the co-immunoprecipitation of two RNAs, (ii) the co-immunoprecipitation of four major polypeptides and (iii) the quantitative immune recognition of both RNase P and RNase MRP. No serum was found that recognizes either one of these two enzymes exclusively.
Walter Rossmanith, Robert Karwan
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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
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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
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RNase P in Research and Therapy [PDF]
Nature Biotechnology, 1995 Fooling the catalytic RNA subunit into recognizing nonnatural substrates may have important implications for ...
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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".
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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".
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Eukaryote RNase P and RNase MRP
2009Ribonuclease 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.
Michael C. Marvin +2 more
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A novel protein shared by RNase MRP and RNase P
RNA (New York, N.Y.), 1997We 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
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Nature structural biology, 2000
In 1989, Sidney Altman and Thomas R. Cech shared the Nobel Prize in Chemistry for their discovery of catalytic properties of RNA. Cech was studying the splicing of RNA in a unicellular organism called Tetrahymena thermophila. He found that the precursor RNA could splice in vitro in the absence of proteins.
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In 1989, Sidney Altman and Thomas R. Cech shared the Nobel Prize in Chemistry for their discovery of catalytic properties of RNA. Cech was studying the splicing of RNA in a unicellular organism called Tetrahymena thermophila. He found that the precursor RNA could splice in vitro in the absence of proteins.
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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.
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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