Interaction of signal-recognition particle 54 GTPase domain and signal-recognition particle RNA in the free signal-recognition particle
about
Structures of the signal recognition particle receptor from the archaeon Pyrococcus furiosus: implications for the targeting step at the membraneStructures of SRP54 and SRP19, the Two Proteins that Organize the Ribonucleic Core of the Signal Recognition Particle from Pyrococcus furiosusStructural basis of signal-sequence recognition by the signal recognition particleThe Structural Basis of FtsY Recruitment and GTPase Activation by SRP RNAUse of synthetic signal sequences to explore the protein export machinery.Exploring the interactions between signal sequences and E. coli SRP by two distinct and complementary crosslinking methodsSignal recognition particle-ribosome binding is sensitive to nascent chain length.Archaea signal recognition particle shows the way.RNA structural motifs that entail hydrogen bonds involving sugar-phosphate backbone atoms of RNA.Allosteric response and substrate sensitivity in peptide binding of the signal recognition particle.Molecular mechanism of co-translational protein targeting by the signal recognition particleProtein targeting by the signal recognition particle.Noncanoncial signal recognition particle RNAs in a major eukaryotic phylum revealed by purification of SRP from the human pathogen Cryptococcus neoformansDynamics of co-translational protein targeting.Breaking on through to the other side: protein export through the bacterial Sec system.Signal recognition particle: an essential protein-targeting machine.Co-translational protein targeting to the bacterial membrane.Fidelity of cotranslational protein targeting by the signal recognition particle.The Archaeal Signal Recognition Particle: Present Understanding and Future Perspective.Domain Organization in the 54-kDa Subunit of the Chloroplast Signal Recognition ParticleDemonstration of a multistep mechanism for assembly of the SRP x SRP receptor complex: implications for the catalytic role of SRP RNA.Signal-sequence induced conformational changes in the signal recognition particle.Conformation of the signal recognition particle in ribosomal targeting complexes.Evolutionary substitution of two amino acids in chloroplast SRP54 of higher plants cause its inability to bind SRP RNA.Structural Changes of RNA in Complex with Proteins in the SRP.Signal sequences get active.Network models reveal stability and structural rearrangement of signal recognition particle.
P2860
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P2860
Interaction of signal-recognition particle 54 GTPase domain and signal-recognition particle RNA in the free signal-recognition particle
description
2007 nî lūn-bûn
@nan
2007 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2007 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
name
Interaction of signal-recognit ...... ee signal-recognition particle
@ast
Interaction of signal-recognit ...... ee signal-recognition particle
@en
Interaction of signal-recognit ...... ee signal-recognition particle
@nl
type
label
Interaction of signal-recognit ...... ee signal-recognition particle
@ast
Interaction of signal-recognit ...... ee signal-recognition particle
@en
Interaction of signal-recognit ...... ee signal-recognition particle
@nl
prefLabel
Interaction of signal-recognit ...... ee signal-recognition particle
@ast
Interaction of signal-recognit ...... ee signal-recognition particle
@en
Interaction of signal-recognit ...... ee signal-recognition particle
@nl
P2093
P2860
P356
P1476
Interaction of signal-recognit ...... ee signal-recognition particle
@en
P2093
A Elisabeth Sauer-Eriksson
Shenghua Huang
Tobias Hainzl
P2860
P304
P356
10.1073/PNAS.0702467104
P407
P577
2007-09-18T00:00:00Z