Modulation of the rate of peptidyl transfer on the ribosome by the nature of substrates.
about
The tmRNA ribosome-rescue systemStructure of the hypusinylated eukaryotic translation factor eIF-5A bound to the ribosomeMultiple Parallel Pathways of Translation Initiation on the CrPV IRESAccounting for biases in riboprofiling data indicates a major role for proline in stalling translation.Genetic identification of nascent peptides that induce ribosome stalling.The 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.eIF5A facilitates translation termination globally and promotes the elongation of many non polyproline-specific tripeptide sequencesThe arginine attenuator peptide interferes with the ribosome peptidyl transferase center.The hypusine-containing translation factor eIF5A.Biochemistry. Getting past polyproline pausesSequence requirements for ribosome stalling by the arginine attenuator peptide.Sequence selectivity of macrolide-induced translational attenuationThe bacterial translation stress response.The non-canonical hydroxylase structure of YfcM reveals a metal ion-coordination motif required for EF-P hydroxylation.Ribosome excursions during mRNA translocation mediate broad branching of frameshift pathwaysDesign of photocaged puromycin for nascent polypeptide release and spatiotemporal monitoring of translation.Nascent peptides that block protein synthesis in bacteria.High-precision analysis of translational pausing by ribosome profiling in bacteria lacking EFP.Translation Control of Swarming Proficiency in Bacillus subtilis by 5-Amino-pentanolylated Elongation Factor PeIF5A promotes translation of polyproline motifs.Distinct XPPX sequence motifs induce ribosome stalling, which is rescued by the translation elongation factor EF-PMaintenance of Transcription-Translation Coupling by Elongation Factor P.Binding of Macrolide Antibiotics Leads to Ribosomal Selection against Specific Substrates Based on Their Charge and Size.Kinetics of paused ribosome recycling in Escherichia coli.Divergent stalling sequences sense and control cellular physiology.Stall no more at polyproline stretches with the translation elongation factors EF-P and IF-5A.Mistakes in translation: Reflections on mechanism.The ribosome in action: Tuning of translational efficiency and protein folding.eIF5A Functions Globally in Translation Elongation and Termination.Induced fit of the peptidyl-transferase center of the ribosome and conformational freedom of the esterified amino acids.Measurement of average decoding rates of the 61 sense codons in vivo.Translational stalling at polyproline stretches is modulated by the sequence context upstream of the stall site.Natural amino acids do not require their native tRNAs for efficient selection by the ribosome.Activities of the peptidyl transferase center of ribosomes lacking protein L27.Molecular insights into protein synthesis with proline residues.EF-P is essential for rapid synthesis of proteins containing consecutive proline residues.Elongation factor P: Function and effects on bacterial fitness.Logical engineering of D-arm and T-stem of tRNA that enhances d-amino acid incorporation.Amino acid substrates impose polyamine, eIF5A, or hypusine requirement for peptide synthesis.
P2860
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P2860
Modulation of the rate of peptidyl transfer on the ribosome by the nature of substrates.
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年学术文章
@wuu
2008年学术文章
@zh
2008年学术文章
@zh-cn
2008年学术文章
@zh-hans
2008年学术文章
@zh-my
2008年学术文章
@zh-sg
2008年學術文章
@yue
2008年學術文章
@zh-hant
name
Modulation of the rate of peptidyl transfer on the ribosome by the nature of substrates.
@en
Modulation of the rate of peptidyl transfer on the ribosome by the nature of substrates.
@nl
type
label
Modulation of the rate of peptidyl transfer on the ribosome by the nature of substrates.
@en
Modulation of the rate of peptidyl transfer on the ribosome by the nature of substrates.
@nl
prefLabel
Modulation of the rate of peptidyl transfer on the ribosome by the nature of substrates.
@en
Modulation of the rate of peptidyl transfer on the ribosome by the nature of substrates.
@nl
P2860
P356
P1476
Modulation of the rate of peptidyl transfer on the ribosome by the nature of substrates.
@en
P2093
Ingo Wohlgemuth
Sibylle Brenner
P2860
P304
32229-32235
P356
10.1074/JBC.M805316200
P407
P577
2008-09-22T00:00:00Z