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Article

Bid binding to negatively charged phospholipids may not be required for its pro-apoptotic activity in vivo.

Biochimica et biophysica acta - 1 Oct 2009

Manara Anna, Lindsay Jennefer, Marchioretto Marta, Astegno Alessandra, Gilmore Andrew P, Esposti Mauro Degli, Crimi Massimo

Abstract excerpt

Bid is a ubiquitous pro-apoptotic member of the Bcl-2 family that has been involved in a variety of pathways of cell death. Unique among pro-apoptotic proteins, Bid is activated after cleavage by the apical caspases of the extrinsic pathway; subsequently it moves to mitochondria, where it promotes the release of apoptogenic proteins in concert with other Bcl-2 family proteins like Bak. Diverse factors appear to...

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Identifiers

PMID: 19463967
DOI: 10.1016/j.bbalip.2009.05.003
PMCID: PMC2822702

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Bid binding to negatively charged phospholipids may not be required for its pro-apoptotic activity in vivo.PMID 19463967Read ↗

Pro-apoptotic Bid induces membrane perturbation by inserting selected lysolipids into the bilayer.Semantic proximity Read ↗

Proapoptotic BID is an ATM effector in the DNA-damage response.Semantic proximity Read ↗

The destabilization of lipid membranes induced by the C-terminal fragment of caspase 8-cleaved bid is inhibited by the N-terminal fragment.Semantic proximity Read ↗

Leakage and aggregation of phospholipid vesicles induced by the BH3-only Bcl-2 family member, BID.Semantic proximity Read ↗

Physiological restraint of Bak by Bcl-xL is essential for cell survival.Semantic proximity Read ↗

The interaction between tBid and cardiolipin or monolysocardiolipin.Semantic proximity Read ↗

BIM and other BCL-2 family proteins exhibit cross-species conservation of function between zebrafish and mammals.Semantic proximity Read ↗

BID-D59A is a potent inducer of apoptosis in primary embryonic fibroblasts.Semantic proximity Read ↗

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

BAK multimerization for apoptosis, but not bid binding, is inhibited by negatively charged residue in the BAK hydrophobic groove.Semantic proximity Read ↗

BID-induced structural changes in BAK promote apoptosis.Semantic proximity Read ↗

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