Evidence map›Paper›PMID 36649479›Full record

ArticleACS synthetic biology2023

Signal Peptide Efficiency: From High-Throughput Data to Prediction and Explanation.

Stefano Grasso, Valentina Dabene, Margriet M W B Hendriks, Priscilla Zwartjens, René Pellaux, Martin Held, Sven Panke, Jan Maarten van Dijl, Andreas Meyer, Tjeerd van Rij

Abstract read
In one paragraph

Article in ACS synthetic biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
–field-weighted citation impact
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

19 citing papers in PubMed.

  1. Review
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  16. Automation-aided construction and characterization ofFrontiers in bioengineering and biotechnology · 2024
    Article
  17. Article
  18. Article
  19. Refined control of CRISPR-Cas9 gene editing inFrontiers in immunology · 2023
    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.

Stefano GrassoDepartment of Medical Microbiology, University of Groningen, University Medical Center Groningen, Hanzeplein 1, Groningen 9700 RB, The Netherlands.
Valentina DabeneDepartment of Biosystems Science and Engineering, ETH Zurich, Mattenstrasse 26, Basel 4058, Switzerland.
Margriet M W B HendriksDSM Biotechnology Center, Alexander Fleminglaan 1, Delft 2613 AX, Netherlands.
Priscilla ZwartjensDSM Biotechnology Center, Alexander Fleminglaan 1, Delft 2613 AX, Netherlands.
René PellauxFGen AG, Hochbergerstrasse 60C, Basel 4057, Switzerland.
Martin HeldDepartment of Biosystems Science and Engineering, ETH Zurich, Mattenstrasse 26, Basel 4058, Switzerland.
Sven PankeDepartment of Biosystems Science and Engineering, ETH Zurich, Mattenstrasse 26, Basel 4058, Switzerland.
Jan Maarten van DijlDepartment of Medical Microbiology, University of Groningen, University Medical Center Groningen, Hanzeplein 1, Groningen 9700 RB, The Netherlands.ORCID 0000-0002-5688-8438
Andreas MeyerFGen AG, Hochbergerstrasse 60C, Basel 4057, Switzerland.
Tjeerd van RijDSM Biotechnology Center, Alexander Fleminglaan 1, Delft 2613 AX, Netherlands.ORCID 0000-0002-0301-2598

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The passage of proteins across biological membranes via the general secretory (Sec) pathway is a universally conserved process with critical functions in cell physiology and important industrial applications. Proteins are directed into the Sec pathway by a signal peptide at their N-terminus. Estimating the impact of physicochemical signal peptide features on protein secretion levels has not been achieved so far, partially due to the extreme sequence variability of signal peptides. To elucidate relevant features of the signal peptide sequence that influence secretion efficiency, an evaluation of ∼12,000 different designed signal peptides was performed using a novel miniaturized high-throughput assay. The results were used to train a machine learning model, and a post-hoc explanation of the model is provided. By describing each signal peptide with a selection of 156 physicochemical features, it is now possible to both quantify feature importance and predict the protein secretion levels directed by each signal peptide. Our analyses allow the detection and explanation of the relevant signal peptide features influencing the efficiency of protein secretion, generating a versatile tool for the de novo design and in silico evaluation of signal peptides.

Indexed as

Bacillus subtilisProtein Sorting SignalsBacterial ProteinsCell MembraneProtein TransportBacterial ProteinsProtein Sorting SignalsamylaseBacillus subtilisnanoliter reactorsprotein secretionsecretion efficiencysignal peptide

Identifiers

PMID36649479
PMCPMC9942255

What OpenQuestion holds

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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.