Evidence map›Paper›PMID 37117294›Full record

ReviewNature reviews. Chemistry2022

Using azobenzene photocontrol to set proteins in motion.

Olga Bozovic, Brankica Jankovic, Peter Hamm

Abstract readReview
PubMed Publisher
In one paragraph

Review in Nature reviews. Chemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing 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

26 citing papers in PubMed.

  1. Photochemical synergy in hybrid sunscreen gels: enhanced UV protection and photostability with algal antioxidants, quercetin, azobenzene, and chitosan-coated TiO₂ nanoparticles.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2026
    Article
  2. Structural Mechanism of an Efficacy Photoswitch Targeting the βAngewandte Chemie (International ed. in English) · 2026
    Article
  3. Review
  4. Review
  5. Article
  6. Near-infrared light-activatedChemical science · 2025
    Article
  7. Article
  8. Effects of binding partners on thermal reversion rates of photoswitchable molecules.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  9. Article
  10. Article
  11. Review
  12. Design of a light and CaProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  13. Substituent effects inBeilstein journal of organic chemistry · 2025
    Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. 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

3 authors.

Olga BozovicDepartment of Chemistry, University of Zurich, Zurich, Switzerland.ORCID 0000-0002-6960-5759
Brankica JankovicDepartment of Chemistry, University of Zurich, Zurich, Switzerland.ORCID 0000-0002-8073-3014
Peter HammDepartment of Chemistry, University of Zurich, Zurich, Switzerland. peter.hamm@chem.uzh.ch.ORCID 0000-0003-1106-6032

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Controlling the activity of proteins with azobenzene photoswitches is a potent tool for manipulating their biological function. With the help of light, it is possible to change binding affinities, control allostery or manipulate complex biological processes, for example. Additionally, owing to their intrinsically fast photoisomerization, azobenzene photoswitches can serve as triggers that initiate out-of-equilibrium processes. Such switching of the activity initiates a cascade of conformational events that can be accessed with time-resolved methods. In this Review, we show how the potency of azobenzene photoswitching can be combined with transient spectroscopic techniques to disclose the order of events and experimentally observe biomolecular interactions in real time. This strategy will further our understanding of how a protein can accommodate, adapt and readjust its structure to answer an incoming signal, revealing more of the dynamical character of proteins.

Indexed as

ProteinsAllosteric SiteAnimalsAzo CompoundsHumansModels, MolecularPeptidesProtein ConformationazobenzeneAzo CompoundsPeptidesProteins

Identifiers

PMID37117294

What OpenQuestion holds

Textmetadata
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.