Evidence map›Paper›PMID 33449370›Full record

ArticleAngewandte Chemie (International ed. in English)2021

Cryo-EM Resolves Molecular Recognition Of An Optojasp Photoswitch Bound To Actin Filaments In Both Switch States.

Sabrina Pospich, Florian Küllmer, Veselin Nasufović, Johanna Funk, Alexander Belyy, Peter Bieling, Hans-Dieter Arndt, Stefan Raunser

Abstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing 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

13 citing papers in PubMed.

  1. Dosing PPARγ Activation With Light Using Fast Relaxing Photoswitches.Angewandte Chemie (International ed. in English) · 2026
    Article
  2. Article
  3. SiR-XActin: A Fluorescent Probe for Imaging Actin Dynamics in Live Cells.Angewandte Chemie (International ed. in English) · 2025
    Article
  4. Article
  5. Review
  6. Next Generation Opto-Jasplakinolides Enable Local Remodeling of Actin Networks.Angewandte Chemie (International ed. in English) · 2022
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Controlling the Covalent Reactivity of a Kinase Inhibitor with Light.Angewandte Chemie (International ed. in English) · 2021
    Article
  12. Total Synthesis and Bioactivity Mapping of Geodiamolide H.Chemistry (Weinheim an der Bergstrasse, Germany) · 2021
    Article
  13. 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

8 authors.

Sabrina PospichDepartment of Structural Biochemistry, Max Planck Institute of Molecular Physiology, Otto-Hahn-Str. 11, 44227, Dortmund, Germany.ORCID 0000-0002-5119-3039
Florian KüllmerInstitute of Organic Chemistry and Macromolecular Chemistry, Friedrich-Schiller-University, Humboldtstr. 10, 07743, Jena, Germany.ORCID 0000-0002-0671-1546
Veselin NasufovićInstitute of Organic Chemistry and Macromolecular Chemistry, Friedrich-Schiller-University, Humboldtstr. 10, 07743, Jena, Germany.ORCID 0000-0001-6812-637X
Johanna FunkDepartment of Systemic Cell Biology, Max Planck Institute of Molecular Physiology, Otto-Hahn-Str. 11, 44227, Dortmund, Germany.ORCID 0000-0003-1214-8531
Alexander BelyyDepartment of Structural Biochemistry, Max Planck Institute of Molecular Physiology, Otto-Hahn-Str. 11, 44227, Dortmund, Germany.ORCID 0000-0003-3106-6574
Peter BielingDepartment of Systemic Cell Biology, Max Planck Institute of Molecular Physiology, Otto-Hahn-Str. 11, 44227, Dortmund, Germany.ORCID 0000-0002-7458-4358
Hans-Dieter ArndtInstitute of Organic Chemistry and Macromolecular Chemistry, Friedrich-Schiller-University, Humboldtstr. 10, 07743, Jena, Germany.ORCID 0000-0002-0792-1422
Stefan RaunserDepartment of Structural Biochemistry, Max Planck Institute of Molecular Physiology, Otto-Hahn-Str. 11, 44227, Dortmund, Germany.ORCID 0000-0001-9373-3016

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Actin is essential for key processes in all eukaryotic cells. Cellpermeable optojasps provide spatiotemporal control of the actin cytoskeleton, confining toxicity and potentially rendering F-actin druggable by photopharmacology. Here, we report cryo electron microscopy (cryo-EM) structures of both isomeric states of one optojasp bound to actin filaments. The high-resolution structures reveal for the first time the pronounced effects of photoswitching a functionalized azobenzene. By characterizing the optojasp binding site and identifying conformational changes within F-actin that depend on the optojasp isomeric state, we refine determinants for the design of functional F-actin photoswitches.

Indexed as

Cryoelectron MicroscopyActin CytoskeletonActinsAzo CompoundsModels, MolecularMolecular ConformationPhotochemical ProcessesActinsazobenzeneAzo Compoundsactin filamentsdrug designelectron microscopyphotoswitchprotein structures

Identifiers

PMID33449370
PMCPMC8048601

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Registered trials

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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.