Results 41 to 50 of about 430,076 (284)
Human serum RNase-L level is inversely associated with metabolic syndrome and age
Background Ribonuclease-L (RNase-L) was known to be a ubiquitous enzyme involved in several cellular functions, especially innate immunity. It was recently shown to participate in adipogenesis in rodents.
Yi-Ting Wang+6 more
doaj +1 more source
RNase P RNA‐mediated cleavage [PDF]
AbstractMetal(II)‐induced hydrolysis of RNA produce products with 5′‐hydroxyls and 2′;3′‐cyclic phosphates at the ends. Ribozymes are RNA molecules that act as catalysts. Some ribozymes that cleave RNA also generate 5′‐hydroxyls and 2′;3′‐cyclic phosphates whereas others produces 5′‐phosphates and 3′‐hydroxyls at the ends of the cleavage products ...
Leif A. Kirsebom, Stefan Trobro
openaire +4 more sources
Antisense-Inhibition der bakteriellen RNase P [PDF]
Ziel der vorliegenden Arbeit war die in vitro- und in vivo-Inhibition bakterieller RNase P mit Antisense-Oligonukleotiden (AS-ON). RNase P ist ein essentielles Ribonukleoproteinenzym, das in allen drei Reichen des Lebens für die Reifung der ptRNAs ...
Grügelsiepe, Heike+1 more
core +1 more source
Evolution and thermodynamics of the slow unfolding of hyperstable monomeric proteins
Background The unfolding speed of some hyperthermophilic proteins is dramatically lower than that of their mesostable homologs. Ribonuclease HII from the hyperthermophilic archaeon Thermococcus kodakaraensis (Tk-RNase HII) is stabilized by its remarkably
Koga Yuichi+8 more
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RNase MRP and RNase P share a common substrate
RNase MRP is a site-specific ribonucleoprotein endoribonuclease that processes RNA from the mammalian mitochondrial displacement loop containing region. RNase P is a site-specific ribonucleoprotein endoribonuclease that processes pre-tRNAs to generate their mature 5'-ends.
Walter Rossmanith+2 more
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Comparative Analysis of Ribonuclease P RNA of the Planctomycetes [PDF]
The planctomycetes, order Planctomycetales, are a distinct phylum of domain Bacteria. Genes encoding the RNA portion of ribonuclease P (RNase P) of some planctomycete members were sequenced and compared with existing database planctomycete sequences ...
Altman+61 more
core +1 more source
Mouse ribonuclease III. cDNA structure, expression analysis, and chromosomal location
Background Members of the ribonuclease III superfamily of double-stranded(ds)-RNA-specific endoribonucleases participate in diverse RNA maturation and decay pathways in eukaryotic and prokaryotic cells. A human RNase III orthologue has been implicated in
Nicholson Rhonda H+2 more
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Phosphatidic acid counteracts S-RNase signaling in pollen by stabilizing the actin cytoskeleton [PDF]
S-RNase is the female determinant of self-incompatibility (SI) in pear (Pyrus bretschneideri). After translocation to the pollen tube, S-RNase degrades rRNA and induces pollen tube death in an S-haplotype-specific manner. In this study, we found that the
Chen, Jianqing+7 more
core +1 more source
Modeling the Thermoproteaceae RNase P RNA [PDF]
The RNA component of the RNase P complex is found throughout most branches of the tree of life and is principally responsible for removing the 5' leader sequence from pre-tRNA transcripts during tRNA maturation. RNase P RNA has a number of universal core features, however variations in sequence and structure found in homologs across the tree of life ...
Todd M. Lowe+2 more
openaire +3 more sources
Ribonuclease P (RNase P) is a class of enzymes involved in the processing of precursor tRNAs to remove their 5'-leader sequences. Ribonuclease P enzymes are classified into two completely distinct classes, i.e.
Yuri Nozawa+3 more
doaj +1 more source