Evidence map›Paper›PMID 33479285›Full record

ArticleScientific reports2021

In vitro synthesis of 32 translation-factor proteins from a single template reveals impaired ribosomal processivity.

Anne Doerr, David Foschepoth, Anthony C Forster, Christophe Danelon

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.4field-weighted citation impact, top 10% 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

24 citing papers in PubMed, 44 citations in OpenAlex.

  1. RfaH licenses RNA polymerase for long-range transcription.bioRxiv : the preprint server for biology · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. A review on computational models for predicting protein solubility.Journal of microbiology (Seoul, Korea) · 2025
    Review
  9. Review
  10. Frontiers in cell and developmental biology · 2025
    Review
  11. Article
  12. Applications of cell free protein synthesis in protein design.Protein science : a publication of the Protein Society · 2024
    Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Review
  19. Investigation of Genome Biology by Synthetic Genome Engineering.Bioengineering (Basel, Switzerland) · 2023
    Review
  20. Advancing synthetic biology through cell-free protein synthesis.Computational and structural biotechnology journal · 2023
    Review
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

4 authors at 2 institutions in 2 countries.

Anne DoerrDepartment of Bionanoscience, Kavli Institute of Nanoscience, Delft University of Technology, Van der Maasweg 9, 2629HZ, Delft, The Netherlands.
David FoschepothDepartment of Bionanoscience, Kavli Institute of Nanoscience, Delft University of Technology, Van der Maasweg 9, 2629HZ, Delft, The Netherlands.
Anthony C ForsterDepartment of Cell and Molecular Biology, Uppsala University, 751 24, Uppsala, Sweden.
Christophe DanelonDepartment of Bionanoscience, Kavli Institute of Nanoscience, Delft University of Technology, Van der Maasweg 9, 2629HZ, Delft, The Netherlands. c.j.a.danelon@tudelft.nl.
Delft University of Technology · NLUppsala University · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Protein synthesis Using Recombinant Elements (PURE) system enables transcription and translation of a DNA template from purified components. Therefore, the PURE system-catalyzed generation of RNAs and proteins constituting the PURE system itself represents a major challenge toward a self-replicating minimal cell. In this work, we show that all translation factors (except elongation factor Tu) and 20 aminoacyl-tRNA synthetases can be expressed in the PURE system from a single plasmid encoding 32 proteins in 30 cistrons. Cell-free synthesis of all 32 proteins is confirmed by quantitative mass spectrometry-based proteomic analysis using isotopically labeled amino acids. We find that a significant fraction of the gene products consists of proteins missing their C-terminal ends. The per-codon processivity loss that we measure lies between 1.3 × 10

Indexed as

Amino AcidsAmino Acyl-tRNA SynthetasesCell-Free SystemCodonDNAEscherichia coliOpen Reading FramesPeptide Elongation Factor TuProtein BiosynthesisProteomicsRecombinant ProteinsRibosomesRNATranscription, GeneticAmino AcidsAmino Acyl-tRNA SynthetasesCodonDNAPeptide Elongation Factor TuRecombinant ProteinsRNA

Identifiers

PMID33479285
PMCPMC7820420
OpenAlexW3123662993

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.