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Article

Bax-induced cytochrome c release from mitochondria depends on alpha-helices-5 and -6.

The Biochemical journal - 15 Feb 2004

Heimlich Gerd, McKinnon Alastair D, Bernardo Katussevani, Brdiczka Dieter, Reed John C, Kain Renate, Krönke Martin, Jürgensmeier Juliane M

Abstract excerpt

The pro-apoptotic protein Bax plays a key role in the mitochondrial signalling pathway. Upon induction of apoptosis, Bax undergoes a conformational change and translocates to mitochondrial membranes, where it inserts and mediates the release of cytochrome c from the intermembrane space into the c...

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Share to bcl-2-Associated X Protein
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 14614769
DOI: 10.1042/BJ20031152
PMCID: PMC1223939

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026. Prepared record publication-14614769-2026-09-01.1. Manifest publication-graph-cohort-2026-09-01.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 1 Sept 2026.

Related research

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Bax-induced cytochrome c release from mitochondria depends on alpha-helices-5 and -6.PMID 14614769Read ↗

Distinct domains control the addressing and the insertion of Bax into mitochondria.Semantic proximity Read ↗

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An optimized high-yield protocol for expression and purification of monomeric full-length BAX proteinSemantic proximity Read ↗

A three-helix homo-oligomerization domain containing BH3 and BH1 is responsible for the apoptotic activity of Bax.Semantic proximity Read ↗

Transmembrane pore formation by the carboxyl terminus of Bax protein.Semantic proximity Read ↗

Translocation of a Bak C-terminus mutant from cytosol to mitochondria to mediate cytochrome C release: implications for Bak and Bax apoptotic function.Semantic proximity Read ↗

Characterization of the anti-apoptotic mechanism of Bcl-B.Semantic proximity Read ↗

Conformational rearrangements in the pro-apoptotic protein, Bax, as it inserts into mitochondria: a cellular death switch.Semantic proximity Read ↗

Bax forms multispanning monomers that oligomerize to permeabilize membranes during apoptosis.Semantic proximity Read ↗

The conformational stability of pro-apoptotic BAX is dictated by discrete residues of the protein core.Semantic proximity Read ↗

The Bax carboxy-terminal hydrophobic helix does not determine organelle-specific targeting but is essential for maintaining Bax in an inactive state and for stable mitochondrial membrane insertion.Semantic proximity Read ↗

Stepwise activation of BAX and BAK by tBID, BIM, and PUMA initiates mitochondrial apoptosis.Semantic proximity Read ↗

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