Evidence map›Paper›PMID 34930833›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2021

Common sequence motifs of nascent chains engage the ribosome surface and trigger factor.

Annika Deckert, Anaïs M E Cassaignau, Xiaolin Wang, Tomasz Włodarski, Sammy H S Chan, Christopher A Waudby, John P Kirkpatrick, Michele Vendruscolo, Lisa D Cabrita, John Christodoulou

Open access · hybridAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.6field-weighted citation impact, top 16% 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

17 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
  2. Article
  3. Structures of protein folding intermediates on the ribosome.Nature structural & molecular biology · 2026
    Article
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  5. Article
  6. Review
  7. Article
  8. Rational design ofNature communications · 2025
    Article
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  15. Article
  16. Cotranslational Biogenesis of Membrane Proteins in Bacteria.Frontiers in molecular biosciences · 2022
    Review
  17. Article
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

10 authors at 2 institutions in 1 country.

Annika DeckertInstitute of Structural and Molecular Biology, University College London, London WC1E 6BT, United Kingdom.ORCID 0000-0002-5280-230X
Anaïs M E CassaignauInstitute of Structural and Molecular Biology, University College London, London WC1E 6BT, United Kingdom; anais.cassaignau.09@ucl.ac.uk j.christodoulou@ucl.ac.uk.ORCID 0000-0003-3963-082X
Xiaolin WangInstitute of Structural and Molecular Biology, University College London, London WC1E 6BT, United Kingdom.ORCID 0000-0002-3370-5053
Tomasz WłodarskiInstitute of Structural and Molecular Biology, University College London, London WC1E 6BT, United Kingdom.ORCID 0000-0001-6498-334X
Sammy H S ChanInstitute of Structural and Molecular Biology, University College London, London WC1E 6BT, United Kingdom.ORCID 0000-0003-1156-1818
Christopher A WaudbyInstitute of Structural and Molecular Biology, University College London, London WC1E 6BT, United Kingdom.ORCID 0000-0001-7810-3753
John P KirkpatrickInstitute of Structural and Molecular Biology, University College London, London WC1E 6BT, United Kingdom.
Michele VendruscoloCentre for Misfolding Disease, University of Cambridge, Cambridge CB2 1EW, United Kingdom.ORCID 0000-0002-3616-1610
Lisa D CabritaInstitute of Structural and Molecular Biology, University College London, London WC1E 6BT, United Kingdom.
John ChristodoulouInstitute of Structural and Molecular Biology, University College London, London WC1E 6BT, United Kingdom; anais.cassaignau.09@ucl.ac.uk j.christodoulou@ucl.ac.uk.
Institute of Structural and Molecular Biology · GBUniversity of Cambridge · GB

Funding

Medical Research Council MC_U117533887Wellcome TrustWellcome Trust 206409/Z/17/Z
6 · The paper itself

Abstract

In the cell, the conformations of nascent polypeptide chains during translation are modulated by both the ribosome and its associated molecular chaperone, trigger factor. The specific interactions that underlie these modulations, however, are still not known in detail. Here, we combine protein engineering, in-cell and in vitro NMR spectroscopy, and molecular dynamics simulations to explore how proteins interact with the ribosome during their biosynthesis before folding occurs. Our observations of α-synuclein nascent chains in living

Indexed as

Escherichia coli ProteinsPeptidesPeptidylprolyl Isomerasealpha-SynucleinAmino Acid MotifsEscherichia coliHumansMagnetic Resonance SpectroscopyMolecular Dynamics SimulationProtein BiosynthesisProtein EngineeringProtein FoldingRibosomesalpha-SynucleinEscherichia coli ProteinsPeptidesPeptidylprolyl IsomeraseSNCA protein, humantrigger factor, E colialpha synucleincotranslational foldingin-cell NMRNMR spectroscopystructural biology

Identifiers

PMID34930833
PMCPMC8719866
OpenAlexW4200177889

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.