Global analysis of chaperone effects using a reconstituted cell-free translation system.
about
Comparing protein folding in vitro and in vivo: foldability meets the fitness challengeEngine out of the chassis: cell-free protein synthesis and its usesMembrane protein production in Escherichia coli cell-free lysatesQuantifying chaperone-mediated transitions in the proteostasis network of E. coliBiochemical Preparation of Cell Extract for Cell-Free Protein Synthesis without Physical DisruptionIdentification of novel in vivo obligate GroEL/ES substrates based on data from a cell-free proteomics approach.Condensation of an additive-free cell extract to mimic the conditions of live cells.Involvement of Escherichia coli DNA Replication Proteins in Phage Lambda Red-Mediated Homologous RecombinationImproved cell-free RNA and protein synthesis system.Protein synthesis using a reconstituted cell-free system.Conceptual and methodological advances in cell-free directed evolution.Comprehensive study of liposome-assisted synthesis of membrane proteins using a reconstituted cell-free translation system.Integrated in vivo and in vitro nascent chain profiling reveals widespread translational pausing.Multifaceted anti-amyloidogenic and pro-amyloidogenic effects of C-reactive protein and serum amyloid P component in vitro.Flexibility of the bacterial chaperone trigger factor in microsecond-timescale molecular dynamics simulations.Lysine and arginine content of proteins: computational analysis suggests a new tool for solubility design.Modulating protein stability - directed evolution strategies for improved protein function.From Gene to Function: Cell-free Electrophysiological and Optical Analysis of Ion Pumps in Nanodiscs.Large-scale analysis of macromolecular crowding effects on protein aggregation using a reconstituted cell-free translation system.Conversion of a chaperonin GroEL-independent protein into an obligate substrate.Cooperative working of bacterial chromosome replication proteins generated by a reconstituted protein expression system.Chaperone addiction of toxin-antitoxin systems.How do eubacterial organisms manage aggregation-prone proteome?A Simple Protein Synthesis Model for the PURE System Operation.Activities of 20 aminoacyl-tRNA synthetases expressed in a reconstituted translation system in Escherichia coli.Genetic engineering modification and fermentation optimization for extracellular production of recombinant proteins using Escherichia coli.In vitro transcription-translation using bacterial genome as a template to reconstitute intracellular profile.Large-scale aggregation analysis of eukaryotic proteins reveals an involvement of intrinsically disordered regions in protein folding.Cotranslational protein assembly imposes evolutionary constraints on homomeric proteins.Multitasking of Hsp70 chaperone in the biogenesis of bacterial functional amyloidsProteoliposome Engineering with Cell-Free Membrane Protein Synthesis: Control of Membrane Protein Sorting into Liposomes by Chaperoning Systems
P2860
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P2860
Global analysis of chaperone effects using a reconstituted cell-free translation system.
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
2012年论文
@zh
2012年论文
@zh-cn
name
Global analysis of chaperone effects using a reconstituted cell-free translation system.
@ast
Global analysis of chaperone effects using a reconstituted cell-free translation system.
@en
type
label
Global analysis of chaperone effects using a reconstituted cell-free translation system.
@ast
Global analysis of chaperone effects using a reconstituted cell-free translation system.
@en
prefLabel
Global analysis of chaperone effects using a reconstituted cell-free translation system.
@ast
Global analysis of chaperone effects using a reconstituted cell-free translation system.
@en
P2860
P356
P1476
Global analysis of chaperone effects using a reconstituted cell-free translation system
@en
P2093
Takashi Kanamori
Tatsuya Niwa
P2860
P304
P356
10.1073/PNAS.1201380109
P407
P577
2012-05-21T00:00:00Z