Molecular mechanism and structure of Trigger Factor bound to the translating ribosome - Wikidata - awgldk - TriplyDB

Molecular mechanism and structure of Trigger Factor bound to the translating ribosome

Molecular mechanism and structure of Trigger Factor bound to the translating ribosome

http://www.wikidata.org/entity/Q27650662

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Chemical and biological approaches for adapting proteostasis to ameliorate protein misfolding and aggregation diseases: progress and prognosis Promiscuous Substrate Recognition in Folding and Assembly Activities of the Trigger Factor Chaperone Crystal Structure of PrgI-SipD: Insight into a Secretion Competent State of the Type Three Secretion System Needle Tip and its Interaction with Host Ligands Structural Basis for Protein Antiaggregation Activity of the Trigger Factor Chaperone Selective ribosome profiling reveals the cotranslational chaperone action of trigger factor in vivo Cotranslational structure acquisition of nascent polypeptides monitored by NMR spectroscopy New structural and functional defects in polyphosphate deficient bacteria: a cellular and proteomic study.Cotranslational folding increases GFP folding yield Lon protease quality control of presecretory proteins in Escherichia coli and its dependence on the SecB and DnaJ (Hsp40) chaperones.The interplay of turn formation and hydrophobic interactions on the early kinetic events in protein folding.Dynamic fluorescence depolarization: a powerful tool to explore protein folding on the ribosome Protein folding in the cytoplasm and the heat shock response.Protein folding at the exit tunnel.High yield expression of catalytically active USP18 (UBP43) using a Trigger Factor fusion system.Hydrophobic collapse of trigger factor monomer in solution Trigger factor from the psychrophilic bacterium Psychrobacter frigidicola is a monomeric chaperone Selective ribosome profiling as a tool for studying the interaction of chaperones and targeting factors with nascent polypeptide chains and ribosomes.Life in the cold: a proteomic study of cold-repressed proteins in the antarctic bacterium pseudoalteromonas haloplanktis TAC125 Regulation by a chaperone improves substrate selectivity during cotranslational protein targeting Conformational dynamics of bacterial trigger factor in apo and ribosome-bound states.Hsp33 controls elongation factor-Tu stability and allows Escherichia coli growth in the absence of the major DnaK and trigger factor chaperones E. coli metabolic protein aldehyde-alcohol dehydrogenase-E binds to the ribosome: a unique moonlighting action revealed Flexibility of the bacterial chaperone trigger factor in microsecond-timescale molecular dynamics simulations.Use of folding modulators to improve heterologous protein production in Escherichia coli.Structural characterization of the interaction of α-synuclein nascent chains with the ribosomal surface and trigger factor Cryo-electron microscopic structure of SecA protein bound to the 70S ribosome.Integrating protein homeostasis strategies in prokaryotes.Cryo-electron microscopy of ribosomal complexes in cotranslational folding, targeting, and translocation.Rewiring translation - Genetic code expansion and its applications.Breaking on through to the other side: protein export through the bacterial Sec system.Fidelity of cotranslational protein targeting by the signal recognition particle.Formyl-methionine as a degradation signal at the N-termini of bacterial proteins.Repair or destruction-an intimate liaison between ubiquitin ligases and molecular chaperones in proteostasis Global Analysis of the Impact of Deleting Trigger Factor on the Transcriptome Profile of Escherichia coli.Acceleration of protein folding by four orders of magnitude through a single amino acid substitution.The molecular timeline of a reviving bacterial spore.Site-specific solid-state NMR studies of "trigger factor" in complex with the large ribosomal subunit 50S.Confined dynamics of a ribosome-bound nascent globin: Cone angle analysis of fluorescence depolarization decays in the presence of two local motions.Versatility of trigger factor interactions with ribosome-nascent chain complexes.Trigger factor lacking the PPIase domain can enhance the folding of eukaryotic multi-domain proteins in Escherichia coli.

P2860

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P2860

Molecular mechanism and structure of Trigger Factor bound to the translating ribosome

http://www.wikidata.org/entity/Q27650662

description

2008 nî lūn-bûn

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2008 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

2008 թվականի հունիսին հրատարակված գիտական հոդված

@hy

2008年の論文

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2008年論文

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2008年論文

@zh-hant

2008年論文

@zh-hk

2008年論文

@zh-mo

2008年論文

@zh-tw

2008年论文

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name

Molecular mechanism and structure of Trigger Factor bound to the translating ribosome

@ast

Molecular mechanism and structure of Trigger Factor bound to the translating ribosome

@en

Molecular mechanism and structure of Trigger Factor bound to the translating ribosome

@nl

type

label

Molecular mechanism and structure of Trigger Factor bound to the translating ribosome

@ast

Molecular mechanism and structure of Trigger Factor bound to the translating ribosome

@en

Molecular mechanism and structure of Trigger Factor bound to the translating ribosome

@nl

prefLabel

Molecular mechanism and structure of Trigger Factor bound to the translating ribosome

@ast

Molecular mechanism and structure of Trigger Factor bound to the translating ribosome

@en

Molecular mechanism and structure of Trigger Factor bound to the translating ribosome

@nl

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P1433

The EMBO Journal

P1476

Molecular mechanism and structure of Trigger Factor bound to the translating ribosome

@en

P2093

Anja Hoffmann

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

Anna Rutkowska

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

Daniel Boehringer

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

Frieder Merz

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

Jasmin Lozza

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

Timm Maier

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

P2860

Structures of the bacterial ribosome at 3.5 A resolution

Molecular chaperones in the cytosol: from nascent chain to folded protein

Folding of newly translated proteins in vivo: the role of molecular chaperones

Exploring the conformational properties of the sequence space between two proteins with different folds: an experimental study.

Getting newly synthesized proteins into shape.

Structure of trigger factor binding domain in biologically homologous complex with eubacterial ribosome reveals its chaperone action

Binding specificity of Escherichia coli trigger factor.

The ribosomal exit tunnel functions as a discriminating gate.

Trigger factor binds to ribosome-signal-recognition particle (SRP) complexes and is excluded by binding of the SRP receptor.

Efficient incorporation of unnatural amino acids into proteins in Escherichia coli.

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1622-32

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scholarly article

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10.1038/EMBOJ.2008.89

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P433

11

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P478

27

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Christiane Schaffitzel

Steffen Preissler

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2008-06-04T00:00:00Z

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5351911

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18497744

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2426727

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