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

Activation of Bax by joint action of tBid and mitochondrial outer membrane: Monte Carlo simulations.

European biophysics journal : EBJ - 1 Sept 2009

Veresov Valery G, Davidovskii Alexander I

Abstract excerpt

The mitochondrial pathway of apoptosis proceeds when molecules, such as cytochrome c, sequestered between the outer and inner mitochondrial membranes are released to the cytosol by mitochondrial outer membrane (MOM) permeabilization. Bax, a member of the Bcl-2 protein family, plays a pivotal role in mitochondrion-mediated apoptosis. In response to apoptotic stimuli, Bax integrates into the MOM, where it mediates...

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 BH3 Interacting Domain Death Agonist Protein

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Binding Sites

Share to Computer Simulation

Share to Membrane Lipids

Share to Mitochondrial Membranes

Share to Monte Carlo Method

Share to Protein Structure, Secondary

Source

Identifiers

PMID: 19466402
DOI: 10.1007/s00249-009-0475-4

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

Activation of Bax by joint action of tBid and mitochondrial outer membrane: Monte Carlo simulations.PMID 19466402Read ↗

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

Computational design of Bax-inhibiting peptidesSemantic proximity Read ↗

100 ns molecular dynamics simulations to study intramolecular conformational changes in Bax.Semantic proximity Read ↗

tBid undergoes multiple conformational changes at the membrane required for Bax activation.Semantic proximity Read ↗

Bax Forms a Membrane Surface Protein-Lipid Complex as it Initiates ApoptosisSemantic proximity Read ↗

Decoding the Heterodimer Stability of Pro-Apoptotic Effectors via Multiscale Simulations: Mutational Insights Into Mitochondrial Signaling.Semantic proximity Read ↗

Oncogenic Mutations Differentially Affect Bax Monomer, Dimer, and Oligomeric Pore Formation in the Membrane.Semantic proximity Read ↗

Mechanistic issues of the interaction of the hairpin-forming domain of tBid with mitochondrial cardiolipin.Semantic proximity Read ↗

Molecular dynamics study of segment peptides of Bax, Bim, and Mcl-1 BH3 domain of the apoptosis-regulating proteins bound to the anti-apoptotic Mcl-1 protein.Semantic proximity Read ↗

Mutation in MCL1 predicted loop to helix structural transition stabilizes MCL1-Bax binding interaction favoring cancer cell survivalSemantic proximity Read ↗

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

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

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