Evidence map›Paper›PMID 20008353›Full record

ArticleThe Journal of biological chemistry2010

Molecular details of Bax activation, oligomerization, and membrane insertion.

Stephanie Bleicken, Mirjam Classen, Pulagam V L Padmavathi, Takashi Ishikawa, Kornelius Zeth, Heinz-Jürgen Steinhoff, Enrica Bordignon

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 95 papers.

0numbers the graph read from it
0cells of the map it votes in
95citing papers in PubMed
4.4field-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

95 citing papers in PubMed, 173 citations in OpenAlex.

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  10. Mitochondrial DNA in cell death and inflammation.Biochemical Society transactions · 2023
    Review
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35 more citing papers are in PubMed but not listed here.

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

7 authors at 3 institutions in 2 countries.

Stephanie BleickenDepartment of Membrane Biochemistry, Max Planck Institute for Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany.
Mirjam Classen
Pulagam V L Padmavathi
Takashi Ishikawa
Kornelius Zeth
Heinz-Jürgen Steinhoff
Enrica Bordignon
ETH Zurich · CHMax Planck Institute of Biochemistry · DEOsnabrück University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Bax and Bid are pro-apoptotic members of the Bcl-2 protein family. Upon cleavage by caspase-8, Bid activates Bax. Activated Bax inserts into the mitochondrial outer membrane forming oligomers which lead to membrane poration, release of cytochrome c, and apoptosis. The detailed mechanism of Bax activation and the topology and composition of the oligomers are still under debate. Here molecular details of Bax activation and oligomerization were obtained by application of several biophysical techniques, including atomic force microscopy, cryoelectron microscopy, and particularly electron paramagnetic resonance (EPR) spectroscopy performed on spin-labeled Bax. Incubation with detergents, reconstitution, and Bid-triggered insertion into liposomes were found to be effective in inducing Bax oligomerization. Bid was shown to activate Bax independently of the stoichiometric ratio, suggesting that Bid has a catalytic function and that the interaction with Bax is transient. The formation of a stable dimerization interface involving two Bcl-2 homology 3 (BH3) domains was found to be the nucleation event for Bax homo-oligomerization. Based on intermolecular distance determined by EPR, a model of six adjacent Bax molecules in the oligomer is presented where the hydrophobic hairpins (helices alpha5 and alpha6) are equally spaced in the membrane and the two BH3 domains are in close vicinity in the dimer interface, separated by >5 nm from the next BH3 pairs.

Indexed as

Protein MultimerizationAnimalsBH3 Interacting Domain Death Agonist ProteinElectron Spin Resonance SpectroscopyMiceMitochondrial MembranesModels, ChemicalProtein ConformationProto-Oncogene Proteins c-bcl-2BH3 Interacting Domain Death Agonist ProteinBid protein, mouseProto-Oncogene Proteins c-bcl-2

Identifiers

PMID20008353
PMCPMC2825459
OpenAlexW2064153659

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.