Chemical engineering of the peptidyl transferase center reveals an important role of the 2'-hydroxyl group of A2451
about
The bacterial ribosome as a target for antibioticsThe chemical versatility of RNAComprehensive genetic selection revealed essential bases in the peptidyl-transferase centerThe transition state for peptide bond formation reveals the ribosome as a water trapIntrinsic pKa values of 3'-N-α-l-aminoacyl-3'-aminodeoxyadenosines determined by pH dependent 1H NMR in H2O.Critical 23S rRNA interactions for macrolide-dependent ribosome stalling on the ErmCL nascent peptide chain.Mechanism of peptide bond synthesis on the ribosome.Mutations of highly conserved bases in the peptidyltransferase center induce compensatory rearrangements in yeast ribosomes.Role of a ribosomal RNA phosphate oxygen during the EF-G-triggered GTP hydrolysis.Fluctuations of transfer RNAs between classical and hybrid statesThe integrity of the G2421-C2395 base pair in the ribosomal E-site is crucial for protein synthesisThe ribosomal peptidyl transferase center: structure, function, evolution, inhibition.Combined Approaches to Site-Specific Modification of RNAContext-specific inhibition of translation by ribosomal antibiotics targeting the peptidyl transferase center.A structural view on the mechanism of the ribosome-catalyzed peptide bond formation.Proximal disruptor aided ligation (ProDAL) of kilobase-long RNAs.Induced fit of the peptidyl-transferase center of the ribosome and conformational freedom of the esterified amino acids.Atomic mutagenesis at the ribosomal decoding site.Transition state chirality and role of the vicinal hydroxyl in the ribosomal peptidyl transferase reaction.Transition states of uncatalyzed hydrolysis and aminolysis reactions of a ribosomal P-site substrate determined by kinetic isotope effects.An intact ribose moiety at A2602 of 23S rRNA is key to trigger peptidyl-tRNA hydrolysis during translation termination.The 2'-OH group of the peptidyl-tRNA stabilizes an active conformation of the ribosomal PTC.The role of the universally conserved A2450-C2063 base pair in the ribosomal peptidyl transferase center.tRNA-derived fragments target the ribosome and function as regulatory non-coding RNA in Haloferax volcanii.A two-step chemical mechanism for ribosome-catalysed peptide bond formation.Oxidative stress damages rRNA inside the ribosome and differentially affects the catalytic center.Atomic mutagenesis of stop codon nucleotides reveals the chemical prerequisites for release factor-mediated peptide release.The ribosome meets synthetic biology.Generation of chemically engineered ribosomes for atomic mutagenesis studies on protein biosynthesis.Essential mechanisms in the catalysis of peptide bond formation on the ribosome.A mechanistic study supports a two-step mechanism for peptide bond formation on the ribosome
P2860
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P2860
Chemical engineering of the peptidyl transferase center reveals an important role of the 2'-hydroxyl group of A2451
description
2005 nî lūn-bûn
@nan
2005 թուականին հրատարակուած գիտական յօդուած
@hyw
2005 թվականին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
Chemical engineering of the pe ...... the 2'-hydroxyl group of A2451
@ast
Chemical engineering of the pe ...... the 2'-hydroxyl group of A2451
@en
Chemical engineering of the pe ...... the 2'-hydroxyl group of A2451
@nl
type
label
Chemical engineering of the pe ...... the 2'-hydroxyl group of A2451
@ast
Chemical engineering of the pe ...... the 2'-hydroxyl group of A2451
@en
Chemical engineering of the pe ...... the 2'-hydroxyl group of A2451
@nl
prefLabel
Chemical engineering of the pe ...... the 2'-hydroxyl group of A2451
@ast
Chemical engineering of the pe ...... the 2'-hydroxyl group of A2451
@en
Chemical engineering of the pe ...... the 2'-hydroxyl group of A2451
@nl
P2093
P2860
P356
P1476
Chemical engineering of the pe ...... the 2'-hydroxyl group of A2451
@en
P2093
Alexander Hüttenhofer
Alexander S Mankin
Brigitte Wotzel
Kathrin Lang
Matthias D Erlacher
Nisha Shankaran
Norbert Polacek
Ronald Micura
P2860
P304
P356
10.1093/NAR/GKI308
P407
P577
2005-01-01T00:00:00Z