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
Regulation of the mevalonate pathway
Goldstein, J. L., & Brown, M. S. (1990) · Nature · doi:10.1038/343425a0 · Cited by 5,394
Cited by
The Bcl2 family: regulators of the cellular life-or-death switch
Cory, S., & Adams, J. M. (2002) · Nature Reviews Cancer · doi:10.1038/nrc883 · Cited by 4,032
(2001) · PubMed · Cited by 2,381
Letai, A., Bassik, M. C., Walensky, L. D., Sorcinelli, M. D., Weiler, S., & Korsmeyer, S. J. (2002) · Cancer Cell · doi:10.1016/s1535-6108(02)00127-7 · Cited by 1,677
Self-citationA Distinct Pathway Remodels Mitochondrial Cristae and Mobilizes Cytochrome c during Apoptosis
Scorrano, L., Ashiya, M., Buttle, K., Weiler, S., Oakes, S. A., Mannella, C. A., & Korsmeyer, S. J. (2002) · Developmental Cell · doi:10.1016/s1534-5807(01)00116-2 · Cited by 1,072
Self-citationTrafficking and signaling by fatty-acylated and prenylated proteins
Resh, M. D. (2006) · Nature Chemical Biology · doi:10.1038/nchembio834 · Cited by 521
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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