Evidence map›Paper›PMID 23818626›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

Kinetic response of a photoperturbed allosteric protein.

Brigitte Buchli, Steven A Waldauer, Reto Walser, Mateusz L Donten, Rolf Pfister, Nicolas Blöchliger, Sandra Steiner, Amedeo Caflisch, Oliver Zerbe, Peter Hamm

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing 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

37 citing papers in PubMed.

  1. Article
  2. Synchronous Rotation Dynamics in a Molecular Motor.Journal of the American Chemical Society · 2026
    Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Sensing the allosteric force.Nature communications · 2020
    Article
  15. Real-time observation of ligand-induced allosteric transitions in a PDZ domain.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  16. Article
  17. Article
  18. Article
  19. Single-molecule FRET methods to study the dynamics of proteins at work.Current opinion in biomedical engineering · 2019
    Article
  20. Allostery in Its Many Disguises: From Theory to Applications.Structure (London, England : 1993) · 2019
    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

10 authors.

Brigitte BuchliDepartment of Chemistry, University of Zurich, CH-8057 Zurich, Switzerland.
Steven A Waldauer
Reto Walser
Mateusz L Donten
Rolf Pfister
Nicolas Blöchliger
Sandra Steiner
Amedeo Caflisch
Oliver Zerbe
Peter Hamm

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

By covalently linking an azobenzene photoswitch across the binding groove of a PDZ domain, a conformational transition, similar to the one occurring upon ligand binding to the unmodified domain, can be initiated on a picosecond timescale by a laser pulse. The protein structures have been characterized in the two photoswitch states through NMR spectroscopy and the transition between them through ultrafast IR spectroscopy and molecular dynamics simulations. The binding groove opens on a 100-ns timescale in a highly nonexponential manner, and the molecular dynamics simulations suggest that the process is governed by the rearrangement of the water network on the protein surface. We propose this rearrangement of the water network to be another possible mechanism of allostery.

Indexed as

LasersModels, MolecularProtein ConformationAllosteric RegulationAzo CompoundsHumansKineticsMagnetic Resonance SpectroscopyMolecular Dynamics SimulationPhotochemistryProtein Tyrosine Phosphatase, Non-Receptor Type 13Spectrophotometry, InfraredTime FactorsWaterazobenzeneAzo CompoundsProtein Tyrosine Phosphatase, Non-Receptor Type 13PTPN13 protein, humanWater

Identifiers

PMID23818626
PMCPMC3718176

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.