Functional equivalence of hairpins in the RNA subunits of RNase MRP and RNase P in Saccharomyces cerevisiae
about
Phylogenetic analysis of the structure of RNase MRP RNA in yeastsSequence analysis of RNase MRP RNA reveals its origination from eukaryotic RNase P RNA.Identification and analysis of ribonuclease P and MRP RNA in a broad range of eukaryotesEukaryotic ribonucleases P/MRP: the crystal structure of the P3 domainInteractions between subunits of Saccharomyces cerevisiae RNase MRP support a conserved eukaryotic RNase P/MRP architecture.Footprinting analysis of interactions between the largest eukaryotic RNase P/MRP protein Pop1 and RNase P/MRP RNA components.Active Yeast Telomerase Shares Subunits with Ribonucleoproteins RNase P and RNase MRPInteractions among the protein and RNA subunits of Saccharomyces cerevisiae nuclear RNase PEukaryotic ribonuclease P: a plurality of ribonucleoprotein enzymesRibozymes, riboswitches and beyond: regulation of gene expression without proteinsRNase MRP and diseaseAn essential protein-binding domain of nuclear RNase P RNA.Ribonuclease P: the evolution of an ancient RNA enzyme.Crystallization and preliminary X-ray diffraction analysis of the P3 RNA domain of yeast ribonuclease MRP in a complex with RNase P/MRP protein components Pop6 and Pop7.Of proteins and RNA: the RNase P/MRP family.Eukaryotic ribonuclease P: increased complexity to cope with the nuclear pre-tRNA pathway.An active precursor in assembly of yeast nuclear ribonuclease P.Substrate recognition by ribonucleoprotein ribonuclease MRP.Specific binding of a Pop6/Pop7 heterodimer to the P3 stem of the yeast RNase MRP and RNase P RNAsFootprinting analysis demonstrates extensive similarity between eukaryotic RNase P and RNase MRP holoenzymes.Identification of a functional core in the RNA component of RNase MRP of budding yeastsModular architecture of eukaryotic RNase P and RNase MRP revealed by electron microscopyRNA affinity tags for purification of RNAs and ribonucleoprotein complexes.The P3 domain of eukaryotic RNases P/MRP: making a protein-rich RNA-based enzyme.Structural organizations of yeast RNase P and RNase MRP holoenzymes as revealed by UV-crosslinking studies of RNA-protein interactions.RNase MRP is required for entry of 35S precursor rRNA into the canonical processing pathway.
P2860
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P2860
Functional equivalence of hairpins in the RNA subunits of RNase MRP and RNase P in Saccharomyces cerevisiae
description
2000 nî lūn-bûn
@nan
2000 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
Functional equivalence of hair ...... P in Saccharomyces cerevisiae
@ast
Functional equivalence of hair ...... P in Saccharomyces cerevisiae
@en
Functional equivalence of hair ...... P in Saccharomyces cerevisiae
@nl
type
label
Functional equivalence of hair ...... P in Saccharomyces cerevisiae
@ast
Functional equivalence of hair ...... P in Saccharomyces cerevisiae
@en
Functional equivalence of hair ...... P in Saccharomyces cerevisiae
@nl
prefLabel
Functional equivalence of hair ...... P in Saccharomyces cerevisiae
@ast
Functional equivalence of hair ...... P in Saccharomyces cerevisiae
@en
Functional equivalence of hair ...... P in Saccharomyces cerevisiae
@nl
P2093
P2860
P1433
P1476
Functional equivalence of hair ...... P in Saccharomyces cerevisiae
@en
P2093
P2860
P304
P356
10.1017/S1355838200992574
P407
P577
2000-05-01T00:00:00Z