The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Posttranslational N-Myristoylation of BID as a Molecular Switch for Targeting Mitochondria and Apoptosis
Abstract
Many apoptotic molecules relocate subcellularly in cells undergoing apoptosis. The pro-apoptotic protein BID underwent posttranslational (rather than classic cotranslational) N-myristoylation when cleavage by caspase 8 caused exposure of a glycine residue. N-myristoylation enabled the targeting of a complex of p7 and myristoylated p15 fragments of BID to artificial membranes bearing the lipid composition of mitochondria, as well as to intact mitochondria. This post-proteolytic N-myristoylation serves as an activating switch, enhancing BID-induced release of cytochrome c and cell death.
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Cites
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Self-citationA Distinct Pathway Remodels Mitochondrial Cristae and Mobilizes Cytochrome c during Apoptosis
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Metadata
- Authors
- Zha, J., Weiler, S., Oh, K. J., Wei, M. C., & Korsmeyer, S. J.
- Venue
- Science
- Published
- 2000-12
- Volume
- 290
- Issue
- 5497
- Pages
- 1761-1765
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2013364831
- Cited by
- 558
- References
- 1
- FWCI
- 12.96
- 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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