Slow peptide bond formation by proline and other N-alkylamino acids in translation - Wikidata - thesis-toulmin - TriplyDB

Slow peptide bond formation by proline and other N-alkylamino acids in translation

Slow peptide bond formation by proline and other N-alkylamino acids in translation

http://www.wikidata.org/entity/Q24646781

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Cell-free biology: exploiting the interface between synthetic biology and synthetic chemistry Structure of the hypusinylated eukaryotic translation factor eIF-5A bound to the ribosome KSHV reactivation and novel implications of protein isomerization on lytic switch control Loss of a conserved tRNA anticodon modification perturbs cellular signaling Neisseria meningitidis Translation Elongation Factor P and Its Active-Site Arginine Residue Are Essential for Cell Viability High-Resolution Analysis of Coronavirus Gene Expression by RNA Sequencing and Ribosome Profiling.Synthetic biology challenges long-held hypotheses in translation, codon bias and transcription.Simulating the pulling of stalled elongated peptide from the ribosome by the translocon.Accounting for biases in riboprofiling data indicates a major role for proline in stalling translation.Ribosome A and P sites revealed by length analysis of ribosome profiling data.Genetic identification of nascent peptides that induce ribosome stalling.Chemical models of peptide formation in translation.The transition state for peptide bond formation reveals the ribosome as a water trap Spatial Distribution and Ribosome-Binding Dynamics of EF-P in Live Escherichia coli.Elevated O₃ enhances the attraction of whitefly-infested tomato plants to Encarsia formosa.SecM-stalled ribosomes adopt an altered geometry at the peptidyl transferase center.Intrinsic pKa values of 3'-N-α-l-aminoacyl-3'-aminodeoxyadenosines determined by pH dependent 1H NMR in H2O.Optimal codon choice can improve the efficiency and fidelity of N-methyl amino acid incorporation into peptides by in-vitro translation.eIF5A facilitates translation termination globally and promotes the elongation of many non polyproline-specific tripeptide sequences Nascentome analysis uncovers futile protein synthesis in Escherichia coli Systematic identification of tRNAome and its dynamics in Lactococcus lactis Asymmetric and non-uniform evolution of recently duplicated human genes.Role of tRNA orthogonality in an expanded genetic code.The hypusine-containing translation factor eIF5A.Translation initiation rate determines the impact of ribosome stalling on bacterial protein synthesis.Biochemistry. Getting past polyproline pauses Sequence selectivity of macrolide-induced translational attenuation pH-sensitivity of the ribosomal peptidyl transfer reaction dependent on the identity of the A-site aminoacyl-tRNA.The bacterial translation stress response.The non-canonical hydroxylase structure of YfcM reveals a metal ion-coordination motif required for EF-P hydroxylation.Ribosome pausing, arrest and rescue in bacteria and eukaryotes.Polyspecific pyrrolysyl-tRNA synthetases from directed evolution Tuning the affinity of aminoacyl-tRNA to elongation factor Tu for optimal decoding The effects of codon context on in vivo translation speed.A novel methodology for enhanced and consistent heterologous expression of unmodified human cytochrome P450 1B1 (CYP1B1).The novel S59P mutation in the TNFRSF1A gene identified in an adult onset TNF receptor associated periodic syndrome (TRAPS) constitutively activates NF-κB pathway Genetic code translation displays a linear trade-off between efficiency and accuracy of tRNA selection Multigene expression in vivo: supremacy of large versus small terminators for T7 RNA polymerase.Distribution of ADAT-Dependent Codons in the Human Transcriptome Mechanisms of SecM-mediated stalling in the ribosome

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P2860

Slow peptide bond formation by proline and other N-alkylamino acids in translation

http://www.wikidata.org/entity/Q24646781

description

2009 nî lūn-bûn

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2009 թուականի Յունուարին հրատարակուած գիտական յօդուած

@hyw

2009 թվականի հունվարին հրատարակված գիտական հոդված

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2009年の論文

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2009年論文

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2009年論文

@zh-hant

2009年論文

@zh-hk

2009年論文

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2009年論文

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2009年论文

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name

Slow peptide bond formation by proline and other N-alkylamino acids in translation

@ast

Slow peptide bond formation by proline and other N-alkylamino acids in translation

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Slow peptide bond formation by proline and other N-alkylamino acids in translation

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type

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Slow peptide bond formation by proline and other N-alkylamino acids in translation

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Slow peptide bond formation by proline and other N-alkylamino acids in translation

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Slow peptide bond formation by proline and other N-alkylamino acids in translation

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prefLabel

Slow peptide bond formation by proline and other N-alkylamino acids in translation

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Slow peptide bond formation by proline and other N-alkylamino acids in translation

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Slow peptide bond formation by proline and other N-alkylamino acids in translation

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PNAS.0809211106

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Proceedings of the National Academy of Sciences of the United States of America

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Slow peptide bond formation by proline and other N-alkylamino acids in translation

@en

P2093

Anthony C Forster

http://www.w3.org/2001/XMLSchema#string

Michael Y Pavlov

http://www.w3.org/2001/XMLSchema#string

Richard E Watts

http://www.w3.org/2001/XMLSchema#string

Virginia W Cornish

http://www.w3.org/2001/XMLSchema#string

Zhongping Tan

http://www.w3.org/2001/XMLSchema#string

P2860

Encodamers: unnatural peptide oligomers encoded in RNA

Uniform binding of aminoacyl-tRNAs to elongation factor Tu by thermodynamic compensation

Messenger RNA-programmed incorporation of multiple N-methyl-amino acids into linear and cyclic peptides

Synthesis of proteins containing modified arginine residues.

Transformation of aminoacyl tRNAs for the in vitro selection of "drug-like" molecules.

Initiation factors IF1 and IF2 synergistically remove peptidyl-tRNAs with short polypeptides from the P-site of translating Escherichia coli ribosomes.

Ribosomal synthesis of unnatural peptides.

Ribosomal synthesis of N-methyl peptides.

Complementary roles of initiation factor 1 and ribosome recycling factor in 70S ribosome splitting.

The kinetics of ribosomal peptidyl transfer revisited.

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50-4

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scholarly article

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1413021

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10.1073/PNAS.0809211106

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1

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106

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Måns Ehrenberg

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2009-01-06T00:00:00Z

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23685669

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19104062

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2629218

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