The P3 domain of eukaryotic RNases P/MRP: making a protein-rich RNA-based enzyme.
about
Conserved regions of ribonucleoprotein ribonuclease MRP are involved in interactions with its substrateFootprinting analysis of interactions between the largest eukaryotic RNase P/MRP protein Pop1 and RNase P/MRP RNA components.Archaeal/eukaryal RNase P: subunits, functions and RNA diversificationInteractions of a Pop5/Rpp1 heterodimer with the catalytic domain of RNase MRP.Modular architecture of eukaryotic RNase P and RNase MRP revealed by electron microscopyStructural organizations of yeast RNase P and RNase MRP holoenzymes as revealed by UV-crosslinking studies of RNA-protein interactions.Crystal Structure of Human Rpp20/Rpp25 Reveals Quaternary Level Adaptation of the Alba Scaffold as Structural Basis for Single-stranded RNA Binding.In vitro reconstitution and analysis of eukaryotic RNase P RNPs.
P2860
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P2860
The P3 domain of eukaryotic RNases P/MRP: making a protein-rich RNA-based enzyme.
description
2010 nî lūn-bûn
@nan
2010年の論文
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2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
2010年论文
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2010年论文
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name
The P3 domain of eukaryotic RNases P/MRP: making a protein-rich RNA-based enzyme.
@en
type
label
The P3 domain of eukaryotic RNases P/MRP: making a protein-rich RNA-based enzyme.
@en
prefLabel
The P3 domain of eukaryotic RNases P/MRP: making a protein-rich RNA-based enzyme.
@en
P2860
P356
P1433
P1476
The P3 domain of eukaryotic RNases P/MRP: making a protein-rich RNA-based enzyme.
@en
P2093
Andrey S Krasilnikov
Anna Perederina
P2860
P304
P356
10.4161/RNA.7.5.12302
P577
2010-09-01T00:00:00Z