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Year Number of Results
1991 1
2001 1
2003 12
2004 22
2005 25
2006 28
2007 30
2008 19
2009 20
2010 27
2011 18
2012 19
2013 12
2014 11
2015 15
2016 19
2017 13
2018 12
2019 3
2020 0
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282 results
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Page 1
Cryo-EM Structure of the Human Ribonuclease P Holoenzyme.
Wu J, et al. Cell 2018. PMID 30454648 Free article.
Ribonuclease (RNase) P is a ubiquitous ribozyme that cleaves the 5' leader from precursor tRNAs. Here, we report cryo-electron microscopy structures of the human nuclear RNase P alone and in complex with tRNA(Val). ...Human RNase P recognizes the tRNA using a double-anchor mechanism through both protein-RNA and RNA-RNA interactions. Structural comparison of the apo and tRNA-bound human RNase P reveals that binding of tRNA induces a local conformational change in the catalytic center, transforming the ribozyme into an active state. ...
Ribonuclease (RNase) P is a ubiquitous ribozyme that cleaves the 5' leader from precursor tRNAs. Here, we report cryo-electron
Structural insight into precursor tRNA processing by yeast ribonuclease P.
Lan P, et al. Science 2018. PMID 30262633
Ribonuclease P (RNase P) is a universal ribozyme responsible for processing the 5'-leader of pre-transfer RNA (pre-tRNA). Here, we report the 3.5-angstrom cryo-electron microscopy structures of Saccharomyces cerevisiae RNase P alone and in complex with pre-tRNA(Phe) The protein components form a hook-shaped architecture that wraps around the RNA and stabilizes RNase P into a "measuring device" with two fixed anchors that recognize the L-shaped pre-tRNA. ...These results not only reveal the architecture of yeast RNase P but also provide a molecular basis of how the 5'-leader of pre-tRNA is processed by eukaryotic RNase P....
Ribonuclease P (RNase P) is a universal ribozyme responsible for processing the 5'-leader of pre-transfer RNA (pre-tRNA
Crystal structure of the ribonuclease-P-protein subunit from Staphylococcus aureus.
Ha L, et al. Acta Crystallogr F Struct Biol Commun 2018. PMID 30279314 Free PMC article.
Staphylococcus aureus ribonuclease-P-protein subunit (RnpA) is a promising antimicrobial target that is a key protein component for two essential cellular processes, RNA degradation and transfer-RNA (tRNA) maturation. ...
Staphylococcus aureus ribonuclease-P-protein subunit (RnpA) is a promising antimicrobial target that is a key protein componen …
Ribonuclease P.
Altman S. Philos Trans R Soc Lond B Biol Sci 2011. PMID 21930585 Free PMC article.
The gene coding for the RNA subunit of ribonuclease P (RNase P) is essential in all free-living organisms. The RNA subunit, itself, is an enzyme and, from its evolutionary tree, we can infer that it is a very ancient molecule. ...
The gene coding for the RNA subunit of ribonuclease P (RNase P) is essential in all free-living organisms. The RNA subu …
The Diversity of Ribonuclease P: Protein and RNA Catalysts with Analogous Biological Functions.
Klemm BP, et al. Biomolecules 2016 - Review. PMID 27187488 Free PMC article.
Ribonuclease P (RNase P) is an essential endonuclease responsible for catalyzing 5' end maturation in precursor transfer RNAs. ...The various RNase P enzymes, in addition to their primary role in tRNA 5' maturation, catalyze cleavage of a variety of alternative substrates, indicating a diversification of RNase P function in vivo. ...
Ribonuclease P (RNase P) is an essential endonuclease responsible for catalyzing 5' end maturation in precursor transfe
Structural basis for activation of an archaeal ribonuclease P RNA by protein cofactors.
Kimura M. Biosci Biotechnol Biochem 2017 - Review. PMID 28715256
Ribonuclease P (RNase P) is an endoribonuclease that catalyzes the processing of the 5'-leader sequence of precursor tRNA (pre-tRNA) in all phylogenetic domains. ...This review describes the structural and functional information on P. horikoshii RNase P, focusing on the structural basis for the PhopRNA activation by the five RNase P proteins....
Ribonuclease P (RNase P) is an endoribonuclease that catalyzes the processing of the 5'-leader sequence of precursor tR
Structural insight into the human mitochondrial tRNA purine N1-methyltransferase and ribonuclease P complexes.
Oerum S, et al. J Biol Chem 2018. PMID 29880640 Free PMC article.
The Mg(2+)-dependent RNase P complex for 5'-end cleavage comprises the methyltransferase domain-containing protein tRNA methyltransferase 10C, mitochondrial RNase P subunit (TRMT10C/MRPP1), short-chain oxidoreductase hydroxysteroid 17β-dehydrogenase 10 (HSD17B10/MRPP2), and metallonuclease KIAA0391/MRPP3. ...The entirety of MRPP1 interacts with MRPP2 to form the N1-methylation complex, whereas the MRPP1-MRPP2-MRPP3 RNase P complex only assembles in the presence of precursor tRNA. ...
The Mg(2+)-dependent RNase P complex for 5'-end cleavage comprises the methyltransferase domain-containing protein tRNA methyltransfe …
Ribozymes
Scott WG. Curr Opin Struct Biol 2007 - Review. PMID 17572081 Free article.
The latest additions include ribonuclease P, group I intron structures, the ribosome (the peptidyl transferase appears to be a ribozyme) and several smaller ribozymes, including a Diels-Alderase, the glmS ribozyme and a new hammerhead ribozyme structure that reconciles 12 years of discord. ...
The latest additions include ribonuclease P, group I intron structures, the ribosome (the peptidyl transferase appears to be a …
Structure of ribonuclease P--a universal ribozyme.
Torres-Larios A, et al. Curr Opin Struct Biol 2006 - Review. PMID 16650980
Ribonuclease P (RNase P) is one of only two known universal ribozymes and was one of the first ribozymes to be discovered. It is involved in RNA processing, in particular the 5' maturation of tRNA. ...Recently, structures of one of the structural domains and of the entire RNA component of RNase P from two different bacteria have been described. ...
Ribonuclease P (RNase P) is one of only two known universal ribozymes and was one of the first ribozymes to be discover
Molecular recognition of pre-tRNA by Arabidopsis protein-only Ribonuclease P.
Klemm BP, et al. RNA 2017. PMID 28874505 Free PMC article.
Protein-only ribonuclease P (PRORP) is an enzyme responsible for catalyzing the 5' end maturation of precursor transfer ribonucleic acids (pre-tRNAs) encoded by various cellular compartments in many eukaryotes. ...
Protein-only ribonuclease P (PRORP) is an enzyme responsible for catalyzing the 5' end maturation of precursor transfer ribonu …
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