Kinetic modelling indicates that fast-translating codons can coordinate cotranslational protein folding by avoiding misfolded intermediates. (Q51125807)

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scientific article published in January 2014

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English	Kinetic modelling indicates that fast-translating codons can coordinate cotranslational protein folding by avoiding misfolded intermediates.	scientific article published in January 2014

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scholarly article

1 reference

Europe PubMed Central

30 March 2018

http://europepmc.org/abstract/MED/24394622

Kinetic modelling indicates that fast-translating codons can coordinate cotranslational protein folding by avoiding misfolded intermediates. (English)

1 reference

Europe PubMed Central

30 March 2018

http://europepmc.org/abstract/MED/24394622

protein folding

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3

object named as

Christopher M Dobson

1 reference

Europe PubMed Central

30 March 2018

Michele Vendruscolo

2

object named as

Michele Vendruscolo

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Europe PubMed Central

30 March 2018

author name string

Edward P O'Brien

1

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Europe PubMed Central

30 March 2018

http://europepmc.org/abstract/MED/24394622

language of work or name

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publication date

1 January 2014

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Europe PubMed Central

30 March 2018

http://europepmc.org/abstract/MED/24394622

Nature Communications

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Europe PubMed Central

30 March 2018

http://europepmc.org/abstract/MED/24394622

5

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Europe PubMed Central

30 March 2018

http://europepmc.org/abstract/MED/24394622

2988

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Europe PubMed Central

30 March 2018

http://europepmc.org/abstract/MED/24394622

https://scigraph.springernature.com/pub.10.1038/ncomms3988

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A pause for thought along the co-translational folding pathway

1 reference

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Slowing bacterial translation speed enhances eukaryotic protein folding efficiency

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Silent substitutions predictably alter translation elongation rates and protein folding efficiencies

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Transient ribosomal attenuation coordinates protein synthesis and co-translational folding.

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Synonymous mutations and ribosome stalling can lead to altered folding pathways and distinct minima

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Non-optimal codon usage affects expression, structure and function of clock protein FRQ

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The efficiency of folding of some proteins is increased by controlled rates of translation in vivo. A hypothesis

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Halting a cellular production line: responses to ribosomal pausing during translation

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Translation drives mRNA quality control

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Mistranslation-induced protein misfolding as a dominant constraint on coding-sequence evolution.

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In vivo translation rates can substantially delay the cotranslational folding of the Escherichia coli cytosolic proteome

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Prediction of variable translation rate effects on cotranslational protein folding.

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Optimizing scaleup yield for protein production: Computationally Optimized DNA Assembly (CODA) and Translation Engineering.

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The anti-Shine-Dalgarno sequence drives translational pausing and codon choice in bacteria

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Evolutionary conservation of codon optimality reveals hidden signatures of cotranslational folding

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An evolutionarily conserved mechanism for controlling the efficiency of protein translation

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FoldEco: a model for proteostasis in E. coli

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An analytical solution to the kinetics of breakable filament assembly

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Trigger factor slows co-translational folding through kinetic trapping while sterically protecting the nascent chain from aberrant cytosolic interactions.

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Alternative to the steady-state method: derivation of reaction rates from first-passage times and pathway probabilities

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A rapid test for identification of autonomous folding units in proteins.

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Single-molecule fluorescence reveals sequence-specific misfolding in multidomain proteins

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Single versus parallel pathways of protein folding and fractional formation of structure in the transition state

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The folding of hen lysozyme involves partially structured intermediates and multiple pathways

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The ribosome as a molecular machine: the mechanism of tRNA-mRNA movement in translocation

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Error bounds for convolutional codes and an asymptotically optimum decoding algorithm

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Structure and dynamics of a ribosome-bound nascent chain by NMR spectroscopy

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The ribosome modulates nascent protein folding

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Principles of protein folding, misfolding and aggregation

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Protein Folding: A Perspective from Theory and Experiment.

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Folding the proteome

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Protein folding rates and stability: how much is there beyond size?

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A "silent" polymorphism in the MDR1 gene changes substrate specificity

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A synonymous single nucleotide polymorphism in DeltaF508 CFTR alters the secondary structure of the mRNA and the expression of the mutant protein

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A novel approach to recovery of function of mutant proteins by slowing down translation.

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Silent mutations affect in vivo protein folding in Escherichia coli

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The importance of sequence diversity in the aggregation and evolution of proteins

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Synonymous codon usage influences the local protein structure observed

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Real-time observation of trigger factor function on translating ribosomes.

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Translationally optimal codons associate with structurally sensitive sites in proteins

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GroEL dependency affects codon usage--support for a critical role of misfolding in gene evolution

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Synonymous but not the same: the causes and consequences of codon bias

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Ribosome-mediated translational pause and protein domain organization

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Heterologous protein expression is enhanced by harmonizing the codon usage frequencies of the target gene with those of the expression host.

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Theory of protein folding

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Theoretical perspectives on protein folding

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Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition

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Statistics of kinetic pathways on biased rough energy landscapes with applications to protein folding.

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Understanding protein folding via free-energy surfaces from theory and experiment

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From macroscopic measurements to microscopic mechanisms of protein aggregation

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Probing ribosome-nascent chain complexes produced in vivo by NMR spectroscopy

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Structural characterization of a misfolded intermediate populated during the folding process of a PDZ domain

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Synonymous codon substitutions affect ribosome traffic and protein folding during in vitro translation

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based on heuristic

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New scenarios of protein folding can occur on the ribosome

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Concerted action of the ribosome and the associated chaperone trigger factor confines nascent polypeptide folding

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Distribution of rare triplets along mRNA and their relation to protein folding

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Identifiers

10.1038/NCOMMS3988

1 reference

Europe PubMed Central

30 March 2018

http://europepmc.org/abstract/MED/24394622

2014NatCo...5.2988O

0 references

1 reference

Europe PubMed Central

30 March 2018

http://europepmc.org/abstract/MED/24394622

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