The critical role of the universally conserved A2602 of 23S ribosomal RNA in the release of the nascent peptide during translation termination.
about
Chemical engineering of the peptidyl transferase center reveals an important role of the 2'-hydroxyl group of A2451Localization of spermine binding sites in 23S rRNA by photoaffinity labeling: parsing the spermine contribution to ribosomal 50S subunit functionsChloramphenicol Derivatives as Antibacterial and Anticancer Agents: Historic Problems and Current SolutionsPeptidyl-CCA deacylation on the ribosome promoted by induced fit and the O3'-hydroxyl group of A76 of the unacylated A-site tRNACrystal structure of a translation termination complex formed with release factor RF2Structure of the 70S ribosome bound to release factor 2 and a substrate analog provides insights into catalysis of peptide releaseBlasticidin S inhibits translation by trapping deformed tRNA on the ribosomeSaccharomyces cerevisiae translational activator Cbs1p is associated with translationally active mitochondrial ribosomes.Synthesis and evaluation of chloramphenicol homodimers: molecular target, antimicrobial activity, and toxicity against human cellsComprehensive genetic selection revealed essential bases in the peptidyl-transferase centertRNA mimicry in translation termination and beyond.Critical 23S rRNA interactions for macrolide-dependent ribosome stalling on the ErmCL nascent peptide chain.A proton wire to couple aminoacyl-tRNA accommodation and peptide-bond formation on the ribosomeCross-linking in the living cell locates the site of action of oxazolidinone antibiotics.Interference probing of rRNA with snoRNPs: a novel approach for functional mapping of RNA in vivoStructural insight into functional aspects of ribosomal RNA targeting.Structure of the Bacillus subtilis 70S ribosome reveals the basis for species-specific stallingRibosomal tolerance and peptide bond formation.From peptide-bond formation to cotranslational folding: dynamic, regulatory and evolutionary aspects.The ribosomal peptidyl transferase center: structure, function, evolution, inhibition.Eukaryotic ribosomal proteins lacking a eubacterial counterpart: important players in ribosomal function.Modulating the activity of the peptidyl transferase center of the ribosome.Structural Basis for Translation Termination on a Pseudouridylated Stop Codon.Uniformity of Peptide Release Is Maintained by Methylation of Release Factors.A structural view on the mechanism of the ribosome-catalyzed peptide bond formation.Functional interactions by transfer RNAs in the ribosome.The ribosomal A site-bound sense and stop codons are similarly positioned towards the A1823-A1824 dinucleotide of the 18S ribosomal RNA.Conjugation with polyamines enhances the antibacterial and anticancer activity of chloramphenicol.Effect of polyamines on the inhibition of peptidyltransferase by antibiotics: revisiting the mechanism of chloramphenicol action.Peptide release on the ribosome depends critically on the 2' OH of the peptidyl-tRNA substrate.A Role for the 2' OH of peptidyl-tRNA substrate in peptide release on the ribosome revealed through RF-mediated rescue.The presence of highly disruptive 16S rRNA mutations in clinical samples indicates a wider role for mutations of the mitochondrial ribosome in human disease.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.rRNA mutants in the yeast peptidyltransferase center reveal allosteric information networks and mechanisms of drug resistance.The role of the universally conserved A2450-C2063 base pair in the ribosomal peptidyl transferase center.Two distinct components of release factor function uncovered by nucleophile partitioning analysis.Oxidative stress damages rRNA inside the ribosome and differentially affects the catalytic center.Unraveling new features of clindamycin interaction with functional ribosomes and dependence of the drug potency on polyamines.Ribosome protection by antibiotic resistance ATP-binding cassette protein.
P2860
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P2860
The critical role of the universally conserved A2602 of 23S ribosomal RNA in the release of the nascent peptide during translation termination.
description
2003 nî lūn-bûn
@nan
2003年の論文
@ja
2003年学术文章
@wuu
2003年学术文章
@zh
2003年学术文章
@zh-cn
2003年学术文章
@zh-hans
2003年学术文章
@zh-my
2003年学术文章
@zh-sg
2003年學術文章
@yue
2003年學術文章
@zh-hant
name
The critical role of the unive ...... uring translation termination.
@en
The critical role of the unive ...... uring translation termination.
@nl
type
label
The critical role of the unive ...... uring translation termination.
@en
The critical role of the unive ...... uring translation termination.
@nl
prefLabel
The critical role of the unive ...... uring translation termination.
@en
The critical role of the unive ...... uring translation termination.
@nl
P2093
P1433
P1476
The critical role of the unive ...... during translation termination
@en
P2093
Alexander Mankin
Koichi Ito
Liqun Xiong
Maria J Gomez
Yoshikazu Nakamura
P304
P356
10.1016/S1097-2765(02)00825-0
P577
2003-01-01T00:00:00Z