Sequence-specific interactions of nascent Escherichia coli polypeptides with trigger factor and signal recognition particle.
about
Molecular mechanism and structure of Trigger Factor bound to the translating ribosomeInsights into the structure and assembly of Escherichia coli outer membrane protein ASelective ribosome profiling reveals the cotranslational chaperone action of trigger factor in vivoMolecular chaperones are nanomachines that catalytically unfold misfolded and alternatively folded proteins.Megadalton complexes in the chloroplast stroma of Arabidopsis thaliana characterized by size exclusion chromatography, mass spectrometry, and hierarchical clusteringAssociation of protein biogenesis factors at the yeast ribosomal tunnel exit is affected by the translational status and nascent polypeptide sequence.Hydrophobic collapse of trigger factor monomer in solutionSecretome of obligate intracellular Rickettsia.Regulation by a chaperone improves substrate selectivity during cotranslational protein targetingThe bacterial Sec-translocase: structure and mechanism.Cotranslational protein folding within the ribosome tunnel influences trigger-factor recruitment.Reprogramming chaperone pathways to improve membrane protein expression in Escherichia coli.YidC is involved in the biogenesis of the secreted autotransporter hemoglobin protease.Escherichia coli SRP, its protein subunit Ffh, and the Ffh M domain are able to selectively limit membrane protein expression when overexpressed.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.High-yield production of recombinant CRM197, a non-toxic mutant of diphtheria toxin, in the periplasm of Escherichia coli.The signal recognition particle contacts uL23 and scans substrate translation inside the ribosomal tunnel.Large-scale purification of ribosome-nascent chain complexes for biochemical and structural studies.Real-time observation of trigger factor function on translating ribosomes.The Bacterial SRP Receptor, SecA and the Ribosome Use Overlapping Binding Sites on the SecY Translocon
P2860
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P2860
Sequence-specific interactions of nascent Escherichia coli polypeptides with trigger factor and signal recognition particle.
description
2006 nî lūn-bûn
@nan
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
2006年论文
@zh
2006年论文
@zh-cn
name
Sequence-specific interactions ...... d signal recognition particle.
@en
type
label
Sequence-specific interactions ...... d signal recognition particle.
@en
prefLabel
Sequence-specific interactions ...... d signal recognition particle.
@en
P2093
P2860
P356
P1476
Sequence-specific interactions ...... d signal recognition particle.
@en
P2093
Bauke Oudega
Edith N G Houben
Joen Luirink
Josef Brunner
Nellie Harms
Ronald S Ullers
P2860
P304
13999-14005
P356
10.1074/JBC.M600638200
P407
P50
P577
2006-03-21T00:00:00Z