Evidence map›Paper›PMID 39455661›Full record

ArticleScientific reports2024

Aligning fermentation conditions with non-canonical amino acid addition strategy is essential for Nε-((2-azidoethoxy)carbonyl)-L-lysine uptake and incorporation into the target protein.

Hana Hanaee-Ahvaz, Marina Alexandra Baumann, Christopher Tauer, Bernd Albrecht, Birgit Wiltschi, Monika Cserjan-Puschmann, Gerald Striedner

Abstract read
In one paragraph

Article in Scientific reports, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. In Vivo Biosynthesis and Direct Incorporation of Noncanonical Amino Acids into Proteins.Chembiochem : a European journal of chemical biology · 2025
    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

7 authors.

Hana Hanaee-AhvazChristian Doppler Laboratory for Production of Next-Level Biopharmaceuticals in E. coli, Department of Biotechnology, BOKU University, Institute of Bioprocess Science and Engineering, Vienna, Austria.
Marina Alexandra BaumannChristian Doppler Laboratory for Production of Next-Level Biopharmaceuticals in E. coli, Department of Biotechnology, BOKU University, Institute of Bioprocess Science and Engineering, Vienna, Austria.
Christopher TauerChristian Doppler Laboratory for Production of Next-Level Biopharmaceuticals in E. coli, Department of Biotechnology, BOKU University, Institute of Bioprocess Science and Engineering, Vienna, Austria.
Bernd AlbrechtBiopharma Austria, Process Science, Boehringer Ingelheim Regional Center Vienna GmbH & Co KG, Vienna, Austria.
Birgit WiltschiChristian Doppler Laboratory for Production of Next-Level Biopharmaceuticals in E. coli, Department of Biotechnology, BOKU University, Institute of Bioprocess Science and Engineering, Vienna, Austria.
Monika Cserjan-PuschmannChristian Doppler Laboratory for Production of Next-Level Biopharmaceuticals in E. coli, Department of Biotechnology, BOKU University, Institute of Bioprocess Science and Engineering, Vienna, Austria. monika.cserjan@boku.ac.at.
Gerald StriednerChristian Doppler Laboratory for Production of Next-Level Biopharmaceuticals in E. coli, Department of Biotechnology, BOKU University, Institute of Bioprocess Science and Engineering, Vienna, Austria.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein engineering with non-canonical amino acids (ncAAs) holds great promises for diverse applications, however, there are still limitations in the implementation of this technology at manufacturing scale. The know-how to efficiently produce ncAA-incorporated proteins in a scalable manner is still very limited. In the present study, we incorporated the ncAA N

Indexed as

Escherichia coliFermentationLysineMethanosarcinaAmino AcidsAmino Acyl-tRNA SynthetasesImmunoglobulin Fab FragmentsProtein EngineeringAmino AcidsAmino Acyl-tRNA SynthetasesImmunoglobulin Fab FragmentsLysineAzk uptakeBench-scaleE. coliFab-functionalized with ncAA

Identifiers

PMID39455661
PMCPMC11511901

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.