Evidence map›Paper›PMID 35858298›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2022

Enhanced incorporation of subnanometer tags into cellular proteins for fluorescence nanoscopy via optimized genetic code expansion.

Tiberiu S Mihaila, Carina Bäte, Lynn M Ostersehlt, Jasmin K Pape, Jan Keller-Findeisen, Steffen J Sahl, Stefan W Hell

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
3.2field-weighted citation impact, top 7% 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

23 citing papers in PubMed, 39 citations in OpenAlex.

  1. Bioorthogonal Chemistry in Neurobiology: From Imaging to Proteomics.Chembiochem : a European journal of chemical biology · 2026
    Review
  2. Chemical reviews · 2026
    Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Journal of microscopy · 2025
    Review
  8. Experimental Approaches to Visualize Effector Protein Translocation During Host-Pathogen Interactions.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025
    Review
  9. Review
  10. Review
  11. Review
  12. Review
  13. Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Bioorthogonal Reactions in Bioimaging.Topics in current chemistry (Cham) · 2024
    Review
  19. Article
  20. 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

7 authors at 2 institutions in 1 country.

Tiberiu S MihailaDepartment of NanoBiophotonics, Max Planck Institute for Multidisciplinary Sciences, Göttingen, 37077, Germany.
Carina BäteDepartment of NanoBiophotonics, Max Planck Institute for Multidisciplinary Sciences, Göttingen, 37077, Germany.
Lynn M OstersehltDepartment of NanoBiophotonics, Max Planck Institute for Multidisciplinary Sciences, Göttingen, 37077, Germany.
Jasmin K PapeDepartment of NanoBiophotonics, Max Planck Institute for Multidisciplinary Sciences, Göttingen, 37077, Germany.
Jan Keller-FindeisenDepartment of NanoBiophotonics, Max Planck Institute for Multidisciplinary Sciences, Göttingen, 37077, Germany.ORCID 0000-0003-2753-0848
Steffen J SahlDepartment of NanoBiophotonics, Max Planck Institute for Multidisciplinary Sciences, Göttingen, 37077, Germany.ORCID 0000-0003-2917-0778
Stefan W HellDepartment of NanoBiophotonics, Max Planck Institute for Multidisciplinary Sciences, Göttingen, 37077, Germany.ORCID 0000-0002-9638-5077
Max Planck Institute for Multidisciplinary SciencesMax Planck Institute for Medical Research · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

With few-nanometer resolution recently achieved by a new generation of fluorescence nanoscopes (MINFLUX and MINSTED), the size of the tags used to label proteins will increasingly limit the ability to dissect nanoscopic biological structures. Bioorthogonal (click) chemical groups are powerful tools for the specific detection of biomolecules. Through the introduction of an engineered aminoacyl-tRNA synthetase/tRNA pair (tRNA: transfer ribonucleic acid), genetic code expansion allows for the site-specific introduction of amino acids with "clickable" side chains into proteins of interest. Well-defined label positions and the subnanometer scale of the protein modification provide unique advantages over other labeling approaches for imaging at molecular-scale resolution. We report that, by pairing a new N-terminally optimized pyrrolysyl-tRNA synthetase (chPylRS

Indexed as

Amino Acyl-tRNA SynthetasesGenetic CodeOptical ImagingRNA, TransferAmino AcidsCell Line, TumorCross-Sectional StudiesFluorescenceHumansAmino AcidsAmino Acyl-tRNA SynthetasesRNA, Transferactinclick chemistryfluorescencegenetic code expansionnanoscopy

Identifiers

PMID35858298
PMCPMC9304028
OpenAlexW4285085410

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.