Evidence map›Paper›PMID 31301980›Full record

ReviewTrends in biochemical sciences2019

Nature and Regulation of Protein Folding on the Ribosome.

Christopher A Waudby, Christopher M Dobson, John Christodoulou

Open access · hybridAbstract readReview
In one paragraph

Review in Trends in biochemical sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 81 papers.

0numbers the graph read from it
0cells of the map it votes in
81citing papers in PubMed
7.1field-weighted citation impact, top 2% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

81 citing papers in PubMed, 155 citations in OpenAlex.

  1. Review
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  5. Structures of protein folding intermediates on the ribosome.Nature structural & molecular biology · 2026
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21 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 3 institutions in 1 country.

Christopher A WaudbyInstitute of Structural and Molecular Biology, University College London and Birkbeck College, London, UK.
Christopher M DobsonCentre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge, UK.
John ChristodoulouInstitute of Structural and Molecular Biology, University College London and Birkbeck College, London, UK. Electronic address: j.christodoulou@ucl.ac.uk.
Birkbeck, University of London · GBInstitute of Structural and Molecular Biology · GBUniversity of Cambridge · GB

Funding

Wellcome Trust 206409/Z/17/Z
6 · The paper itself

Abstract

Co-translational protein folding is an essential process by which cells ensure the safe and efficient production and assembly of new proteins in their functional native states following biosynthesis on the ribosome. In this review, we describe recent progress in probing the changes during protein synthesis of the free energy landscapes that underlie co-translational folding and discuss the critical coupling between these landscapes and the rate of translation that ultimately determines the success or otherwise of the folding process. Recent developments have revealed a variety of mechanisms by which both folding and translation can be modulated or regulated, and we discuss how these effects are utilised by the cell to optimise the outcome of protein biosynthesis.

Indexed as

Protein BiosynthesisProtein FoldingAnimalsHumansKineticsModels, MolecularMolecular ChaperonesProtein ConformationRibosomesThermodynamicsMolecular Chaperonesco-translational foldingfree energy landscapemolecular chaperonesprotein synthesistranslation kinetics

Identifiers

PMID31301980
PMCPMC7471843
OpenAlexW2960982755

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.