From structure and dynamics of protein L7/L12 to molecular switching in ribosome
about
Solution structure of the dimerization domain of the eukaryotic stalk P1/P2 complex reveals the structural organization of eukaryotic stalk complexFunctional Importance of Mobile Ribosomal ProteinsStructural Basis for Translation Factor Recruitment to the Eukaryotic/Archaeal RibosomesSolution structure of the dimerization domain of ribosomal protein P2 provides insights for the structural organization of eukaryotic stalkHead swivel on the ribosome facilitates translocation by means of intra-subunit tRNA hybrid sitesBuckwheat trypsin inhibitor with helical hairpin structure belongs to a new family of plant defence peptidesSolution structure of human P1*P2 heterodimer provides insights into the role of eukaryotic stalk in recruiting the ribosome-inactivating protein trichosanthin to the ribosomeInteractions of an essential Bacillus subtilis GTPase, YsxC, with ribosomesExploring global motions and correlations in the ribosome.A novel dimeric structure of the RimL Nalpha-acetyltransferase from Salmonella typhimurium.Mass spectrometry of hydrogen/deuterium exchange in 70S ribosomal proteins from E. coli.Structural basis for the interaction of protein S1 with the Escherichia coli ribosome.Functional divergence between the two P1-P2 stalk dimers on the ribosome in their interaction with ricin A chainHuman ribosomal P1-P2 heterodimer represents an optimal docking site for ricin A chain with a prominent role for P1 C-terminus.Bacterial ribosome requires multiple L12 dimers for efficient initiation and elongation of protein synthesis involving IF2 and EF-G.EF-G and EF4: translocation and back-translocation on the bacterial ribosome.Altered regulation of the OmpF porin by Fis in Escherichia coli during an evolution experiment and between B and K-12 strains.Elastic properties of ribosomal RNA building blocks: molecular dynamics of the GTPase-associated center rRNAYeast ribosomal stalk heterogeneity in vivo shown by two-photon FCS and molecular brightness analysis.MDMX contains an autoinhibitory sequence element.Comprehensive analysis of phosphorylated proteins of Escherichia coli ribosomes.Charge segregation and low hydrophobicity are key features of ribosomal proteins from different organisms.Protein folding on the ribosome studied using NMR spectroscopy.Stability of the 'L12 stalk' in ribosomes from mesophilic and (hyper)thermophilic Archaea and Bacteria.The ribosome and its role in protein folding: looking through a magnifying glass.Structure and Dynamics of Ribosomal Protein L12: An Ensemble Model Based on SAXS and NMR Relaxation.Mechanism and rates of exchange of L7/L12 between ribosomes and the effects of binding EF-G.Combining NMR and small angle X-ray scattering for the study of biomolecular structure and dynamics.Ribosomal protein L7/L12 is required for GTPase translation factors EF-G, RF3, and IF2 to bind in their GTP state to 70S ribosomes.A single-step method for purification of active His-tagged ribosomes from a genetically engineered Escherichia coliMolecular insights into the interaction of the ribosomal stalk protein with elongation factor 1α.Functional interaction between bases C1049 in domain II and G2751 in domain VI of 23S rRNA in Escherichia coli ribosomes.The N-terminal regions of eukaryotic acidic phosphoproteins P1 and P2 are crucial for heterodimerization and assembly into the ribosomal GTPase-associated center.Control of phosphate release from elongation factor G by ribosomal protein L7/12.The ribosome structure controls and directs mRNA entry, translocation and exit dynamicsThree binding sites for stalk protein dimers are generally present in ribosomes from archaeal organism.Transcription-translation coupling: direct interactions of RNA polymerase with ribosomes and ribosomal subunits.Engineering and characterization of the ribosomal L10.L12 stalk complex. A structural element responsible for high turnover of the elongation factor G-dependent GTPase.HYCUD: a computational tool for prediction of effective rotational correlation time in flexible proteins.Multiplication of Ribosomal P-Stalk Proteins Contributes to the Fidelity of Translation.
P2860
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P2860
From structure and dynamics of protein L7/L12 to molecular switching in ribosome
description
2004 nî lūn-bûn
@nan
2004 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
From structure and dynamics of protein L7/L12 to molecular switching in ribosome
@ast
From structure and dynamics of protein L7/L12 to molecular switching in ribosome
@en
From structure and dynamics of protein L7/L12 to molecular switching in ribosome
@nl
type
label
From structure and dynamics of protein L7/L12 to molecular switching in ribosome
@ast
From structure and dynamics of protein L7/L12 to molecular switching in ribosome
@en
From structure and dynamics of protein L7/L12 to molecular switching in ribosome
@nl
prefLabel
From structure and dynamics of protein L7/L12 to molecular switching in ribosome
@ast
From structure and dynamics of protein L7/L12 to molecular switching in ribosome
@en
From structure and dynamics of protein L7/L12 to molecular switching in ribosome
@nl
P2093
P2860
P356
P1476
From structure and dynamics of protein L7/L12 to molecular switching in ribosome
@en
P2093
Alexander G Sobol
Alexander S Arseniev
Anatoly T Gudkov
Dmitry M Korzhnev
Eduard V Bocharov
Victor A Jaravine
P2860
P304
17697-17706
P356
10.1074/JBC.M313384200
P407
P577
2004-02-11T00:00:00Z