Evidence map›Paper›PMID 37027152›Full record

ReviewProtein science : a publication of the Protein Society2023

Genetically encoded crosslinkers to address protein-protein interactions.

Yasmin Aydin, Irene Coin

Open access · hybridAbstract readReview
In one paragraph

Review in Protein science : a publication of the Protein Society, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
4.2field-weighted citation impact, top 5% 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

21 citing papers in PubMed, 28 citations in OpenAlex.

  1. Review
  2. Evolutionarily conserved hydrophobicity and sterics in TM3/TM4 balance Orai1 pore opening.Protein science : a publication of the Protein Society · 2026
    Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Article
  9. Recent advances in the expanding genetic code.Current opinion in chemical biology · 2024
    Review
  10. Review
  11. Review
  12. Review
  13. Review
  14. Review
  15. Review
  16. Kinase-catalyzed crosslinking: A comparison of ATP-crosslinker analogs.Bioorganic & medicinal chemistry letters · 2024
    Article
  17. Review
  18. Non-Canonical Amino Acids in Analyses of Protease Structure and Function.International journal of molecular sciences · 2023
    Review
  19. Article
  20. Genetically encoded crosslinkers to address protein-protein interactions.Protein science : a publication of the Protein Society · 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

2 authors at 1 institution in 1 country.

Yasmin AydinFaculty of Life Science, Institute of Biochemistry, Leipzig University, Leipzig, Germany.ORCID 0000-0003-0024-7428
Irene CoinFaculty of Life Science, Institute of Biochemistry, Leipzig University, Leipzig, Germany.ORCID 0000-0002-7722-004X
Leipzig University of Applied Sciences · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Noncanonical amino acids (ncAAs) for photo- and chemical crosslinking are powerful biochemical tools for studying and manipulating interactions between proteins both in vitro and in intact cells. Since the first crosslinking ncAAs were genetically encoded about 20 years ago, the technology has now ripened beyond the proof-of-principle demonstrations and is contributing to the study of relevant biological questions in the frame of modern integrative approaches. Here, we provide an overview of available photo-activatable ncAAs for photo-crosslinking and electrophilic ncAAs for genetically encoded chemical crosslinking (GECX), with a major focus on the most recent entries such as ncAAs for SuFEx click chemistry and photo-activatable ncAAs for chemical crosslinking. We present recent examples of the application of genetically encoded crosslinkers to capture protein-protein interactions and identify interaction partners in live cells, to investigate molecular mechanisms of protein function, to stabilize protein complexes for structural studies, to derive structural information about protein complexes from the physiological cell environment, up to perspective applications of GECX-ncAAs for the development of covalent drugs.

Indexed as

Amino AcidsProteinsCross-Linking ReagentsAmino AcidsCross-Linking ReagentsProteinsaffinity crosslinkinggenetically encoded chemical crosslinkersgenetic code expansionlive-cell crosslinkingphoto-crosslinkingprotein-protein interactionsunnatural amino acids

Identifiers

PMID37027152
PMCPMC10117390
OpenAlexW4362691845

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.