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Mechanisms of CFTR Folding at the Endoplasmic ReticulumDecoding mechanisms by which silent codon changes influence protein biogenesis and functionMacromolecule-assisted de novo protein foldingComparing protein folding in vitro and in vivo: foldability meets the fitness challengeA structural ensemble of a ribosome-nascent chain complex during cotranslational protein folding.Ribosomal Stalk Protein Silencing Partially Corrects the ΔF508-CFTR Functional Expression DefectA comparison of the folding characteristics of free and ribosome-tethered polypeptide chains using limited proteolysis and mass spectrometryCapturing the mechanical unfolding pathway of a large protein with coiled-coil probes.High-resolution optical tweezers for single-molecule manipulation.Signal recognition particle-ribosome binding is sensitive to nascent chain length.Cotranslational Protein Folding inside the Ribosome Exit Tunnel.Single-molecule force spectroscopy reveals force-enhanced binding of calcium ions by gelsolinChaperones rescue luciferase folding by separating its domains.In vivo translation rates can substantially delay the cotranslational folding of the Escherichia coli cytosolic proteomeMechanisms of cellular proteostasis: insights from single-molecule approachesGenetic code-guided protein synthesis and folding in Escherichia coli.Revealing -1 programmed ribosomal frameshifting mechanisms by single-molecule techniques and computational methodsNanomanipulation of single RNA molecules by optical tweezers.Reconstitution of translation from Thermus thermophilus reveals a minimal set of components sufficient for protein synthesis at high temperatures and functional conservation of modern and ancient translation componentsIdentical RNA-protein interactions in vivo and in vitro and a scheme of folding the newly synthesized proteins by ribosomes.Single-Molecule Chemo-Mechanical Spectroscopy Provides Structural Identity of Folding Intermediates.Autotransporters: The Cellular Environment Reshapes a Folding Mechanism to Promote Protein TransportStructural characterization of the interaction of α-synuclein nascent chains with the ribosomal surface and trigger factorA transformation for the mechanical fingerprints of complex biomolecular interactions.Quantitative determination of ribosome nascent chain stability.Probing the mechanisms of translation with force.Protein folding on the ribosome studied using NMR spectroscopy.Studying genomic processes at the single-molecule level: introducing the tools and applications.Synonymous Codons Direct Cotranslational Folding toward Different Protein Conformations.Accurate prediction of cellular co-translational folding indicates proteins can switch from post- to co-translational foldingDecoding the mechanical fingerprints of biomolecules.Designing disorder: Tales of the unexpected tails.The ribosome in action: Tuning of translational efficiency and protein folding.Stability of RNA quadruplex in open reading frame determines proteolysis of human estrogen receptor α.Synonymous Codons: Choose Wisely for Expression.Hidden Markov Modeling with Detailed Balance and Its Application to Single Protein Folding.The chaperone toolbox at the single-molecule level: From clamping to confining.Folding of proteins with a flavodoxin-like architecture.The Ribosome Restrains Molten Globule Formation in Stalled Nascent FlavodoxinConformational Dynamics of mRNA in Gene Expression as New Pharmaceutical Target.
P2860
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P2860
description
2011 nî lūn-bûn
@nan
2011年の論文
@ja
2011年学术文章
@wuu
2011年学术文章
@zh-cn
2011年学术文章
@zh-hans
2011年学术文章
@zh-my
2011年学术文章
@zh-sg
2011年學術文章
@yue
2011年學術文章
@zh
2011年學術文章
@zh-hant
name
The ribosome modulates nascent protein folding.
@en
The ribosome modulates nascent protein folding.
@nl
type
label
The ribosome modulates nascent protein folding.
@en
The ribosome modulates nascent protein folding.
@nl
prefLabel
The ribosome modulates nascent protein folding.
@en
The ribosome modulates nascent protein folding.
@nl
P2093
P2860
P356
P1433
P1476
The ribosome modulates nascent protein folding.
@en
P2093
Christian M Kaiser
Daniel H Goldman
Ignacio Tinoco
P2860
P304
P356
10.1126/SCIENCE.1209740
P407
P577
2011-12-01T00:00:00Z