Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Substitutions of potentially phosphorylatable serine residues of Bax reveal how they may regulate its interaction with mitochondria.

The Journal of biological chemistry - 30 Nov 2007

Arokium Hubert, Ouerfelli Hakim, Velours Gisèle, Camougrand Nadine, Vallette François M, Manon Stéphen

Abstract excerpt

During apoptosis, the pro-apoptotic protein Bax relocalizes from the cytosol to the mitochondrial outer membrane. This relocalization is associated to major conformational changes, namely at the N- and C-terminal ends of the protein. Substitution of residues located at critical positions within the protein potentially stimulates or inhibits this process. In the present study, we investigated the hypothesis that...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to bcl-2-Associated X Protein
Share to Fungal Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Glycogen Synthase Kinase 3

Share to Glycogen Synthase Kinase 3 beta

Share to Mitochondria

Share to Protein Transport

Share to Proto-Oncogene Proteins c-akt

Share to Serine

Source

Identifiers

PMID: 17911107
DOI: 10.1074/jbc.M704891200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Substitutions of potentially phosphorylatable serine residues of Bax reveal how they may regulate its interaction with mitochondria.PMID 17911107Read ↗

Mono- or double-site phosphorylation distinctly regulates the proapoptotic function of Bax.Semantic proximity Read ↗

Regulation of Bax/mitochondria interaction by AKT.Semantic proximity Read ↗

Conformation of the Bax C-terminus regulates subcellular location and cell death.Semantic proximity Read ↗

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

Involvement of the N-terminus of Bax in its intracellular localization and function.Semantic proximity Read ↗

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

Serine 162, an essential residue for the mitochondrial localization, stability and anti-apoptotic function of Mcl-1.Semantic proximity Read ↗

Phosphorylation switches Bax from promoting to inhibiting apoptosis thereby increasing drug resistance.Semantic proximity Read ↗

The substitution of Proline 168 favors Bax oligomerization and stimulates its interaction with LUVs and mitochondria.Semantic proximity Read ↗

Physiological and Pharmacological Control of BAK, BAX, and BeyondSemantic proximity Read ↗

Phosphorylation of specific serine residues in the PKR activation domain of PACT is essential for its ability to mediate apoptosis.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 ↗

⌁Select a neighboring publication to make it the new centre.