Evidence map›Paper›PMID 25458844›Full record

ArticleMolecular cell2014

Structural model of active Bax at the membrane.

Stephanie Bleicken, Gunnar Jeschke, Carolin Stegmueller, Raquel Salvador-Gallego, Ana J García-Sáez, Enrica Bordignon

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 118 papers.

0numbers the graph read from it
0cells of the map it votes in
118citing papers in PubMed
34.8field-weighted citation impact, top 1% 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

118 citing papers in PubMed, 222 citations in OpenAlex.

  1. AFM to Study Pore-Forming Proteins.Methods in molecular biology (Clifton, N.J.) · 2027
    Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Review
  7. Review
  8. Review
  9. Article
  10. Protein Modeling with DEER Spectroscopy.Annual review of biophysics · 2025
    Review
  11. Article
  12. Review
  13. Review
  14. Review
  15. Article
  16. Review
  17. Mechanisms of BCL-2 family proteins in mitochondrial apoptosis.Nature reviews. Molecular cell biology · 2023
    Review
  18. Article
  19. Article
  20. Review

58 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 2 countries.

Stephanie BleickenMax Planck Institute for Intelligent Systems, Heisenbergstrasse 3, 70569 Stuttgart, Germany; German Cancer Research Center, Im Neuenheimer Feld 267, 69120 Heidelberg, Germany; Interfaculty Institute of Biochemistry, Eberhard Karls University Tübingen, Hoppe-Seyler-Strasse 4, 72076 Tübingen, Germany.
Gunnar JeschkeLaboratory of Physical Chemistry, ETH Zurich, Vladimir-Prelog-Weg 2, 8093 Zurich, Switzerland.
Carolin StegmuellerMax Planck Institute for Intelligent Systems, Heisenbergstrasse 3, 70569 Stuttgart, Germany; German Cancer Research Center, Im Neuenheimer Feld 267, 69120 Heidelberg, Germany; Interfaculty Institute of Biochemistry, Eberhard Karls University Tübingen, Hoppe-Seyler-Strasse 4, 72076 Tübingen, Germany.
Raquel Salvador-GallegoMax Planck Institute for Intelligent Systems, Heisenbergstrasse 3, 70569 Stuttgart, Germany; German Cancer Research Center, Im Neuenheimer Feld 267, 69120 Heidelberg, Germany; Interfaculty Institute of Biochemistry, Eberhard Karls University Tübingen, Hoppe-Seyler-Strasse 4, 72076 Tübingen, Germany.
Ana J García-SáezMax Planck Institute for Intelligent Systems, Heisenbergstrasse 3, 70569 Stuttgart, Germany; German Cancer Research Center, Im Neuenheimer Feld 267, 69120 Heidelberg, Germany; Interfaculty Institute of Biochemistry, Eberhard Karls University Tübingen, Hoppe-Seyler-Strasse 4, 72076 Tübingen, Germany. Electronic address: ana.garcia@uni-tuebingen.de.
Enrica BordignonLaboratory of Physical Chemistry, ETH Zurich, Vladimir-Prelog-Weg 2, 8093 Zurich, Switzerland; Fachbereich Physik, Freie Universität Berlin, Arnimallee 14, 14195 Berlin, Germany. Electronic address: enrica.bordignon@fu-berlin.de.
German Cancer Research Center · DEETH Zurich · CH

Funding

European Research Council 309966
6 · The paper itself

Abstract

Bax plays a central role in the mitochondrial pathway of apoptosis. Upon activation, cytosolic Bax monomers oligomerize on the surface of mitochondria and change conformation concertedly to punch holes into the outer membrane. The subsequent release of cytochrome c initiates cell death. However, the structure of membrane-inserted Bax and its mechanism of action remain largely unknown. Here, we propose a 3D model of active Bax at the membrane based on double electron-electron resonance (DEER) spectroscopy in liposomes and isolated mitochondria. We show that active Bax is organized at the membrane as assemblies of dimers. In addition to a stable dimerization domain, each monomer contains a more flexible piercing domain involved in interdimer interactions and pore formation. The most important structural change during Bax activation is the opening of the hairpin formed by helices 5 and 6, which adopts a clamp-like conformation central to the mechanism of mitochondrial permeabilization.

Indexed as

Animalsbcl-2-Associated X ProteinCell MembraneMiceModels, MolecularProtein MultimerizationProtein Structure, QuaternaryProtein Structure, SecondaryProtein Structure, Tertiarybcl-2-Associated X Protein

Identifiers

PMID25458844
PMCPMC4869853
OpenAlexW1979471022

What OpenQuestion holds

Textmetadata
LicenceTDM
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.