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Cited by 1,028

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

Inhibition of Bax Channel-Forming Activity by Bcl-2

Antonsson, Bruno, Conti, Franco, Ciavatta, AnnaMaria, Montessuit, Sylvie, Lewis, Shareta, Martinou, Isabelle, Bernasconi, Lilia, Bernard, Alain, Mermod, Jean-Jacques, Mazzei, Gonzalo, Maundrell, Kinsey, Gambale, Franco, Sadoul, Rémy, Martinou, Jean-Claude·1997·Science

Abstract

Proteins of the Bcl-2 family are intracellular membrane-associated proteins that regulate programmed cell death (apoptosis) either positively or negatively by as yet unknown mechanisms. Bax, a pro-apoptotic member of the Bcl-2 family, was shown to form channels in lipid membranes. Bax triggered the release of liposome-encapsulated carboxyfluorescein at both neutral and acidic pH. At physiological pH, release could be blocked by Bcl-2. Bcl-2, in contrast, triggered carboxyfluorescein release at acidic pH only. In planar lipid bilayers, Bax formed pH- and voltage-dependent ion-conducting channels. Thus, the pro-apoptotic effects of Bax may be elicited through an intrinsic pore-forming activity that can be antagonized by Bcl-2.

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Crossref · 10.1126/science.277.5324.370

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Metadata

Authors
Antonsson, B., Conti, F., Ciavatta, A., Montessuit, S., Lewis, S., Martinou, I., Bernasconi, L., Bernard, A., Mermod, J.-J., Mazzei, G., Maundrell, K., Gambale, F., Sadoul, R., & Martinou, J.-C.
Venue
Science
Published
1997-07-18
Volume
277
Issue
5324
Pages
370-372
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2161641464
Cited by
1,028
References
1
FWCI
32.06
Type
journal article
Language
en
Open access
closed

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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