The DOI matches its Crossref record; 30 of the 31 references it cites were found in a registry or an index.
Activation of Apoptosis in Vivo by a Hydrocarbon-Stapled BH3 Helix
Open accessAbstract
BCL-2 family proteins constitute a critical control point for the regulation of apoptosis. Protein interaction between BCL-2 members is a prominent mechanism of control and is mediated through the amphipathic α-helical BH3 segment, an essential death domain. We used a chemical strategy, termed hydrocarbon stapling, to generate BH3 peptides with improved pharmacologic properties. The stapled peptides, called “stabilized alpha-helix of BCL-2 domains” (SAHBs), proved to be helical, protease-resistant, and cell-permeable molecules that bound with increased affinity to multidomain BCL-2 member pockets. A SAHB of the BH3 domain from the BID protein specifically activated the apoptotic pathway to kill leukemia cells. In addition, SAHB effectively inhibited the growth of human leukemia xenografts in vivo. Hydrocarbon stapling of native peptides may provide a useful strategy for experimental and therapeutic modulation of protein-protein interactions in many signaling pathways.
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Cites
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An inhibitor of Bcl-2 family proteins induces regression of solid tumours
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Metadata
- Authors
- Walensky, L. D., Kung, A. L., Escher, I., Malia, T. J., Barbuto, S., Wright, R. D., Wagner, G., Verdine, G. L., & Korsmeyer, S. J.
- Affiliations
- Boston Children's Hospital (US)
- Corresponding author
- Verdine, Gregory L.
- Korsmeyer, Stanley J.
- Venue
- Science
- Published
- 2004-09-03
- Volume
- 305
- Issue
- 5689
- Pages
- 1466-1470
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- PMC
- PMC1360987
- OpenAlex
- W2008845432
- Cited by
- 1,349
- References
- 31
- Citations by year
- 2026: 27 · 2025: 43 · 2024: 48 · 2023: 45 · 2022: 43 · 2021: 49 · 2020: 55 · 2019: 67 · 2018: 50 · 2017: 71 · 2016: 75 · 2015: 85 · 2014: 77 · 2013: 86 · 2012: 78
- FWCI
- 21.43
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Heart, Lung, and Blood Institute (K08HL074049)
- National Cancer Institute (R37 CA50239, R37CA050239)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Physical Sciences › Chemistry › Organic Chemistry › Chemical Synthesis and Analysis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Degradation and Inhibitors
- Keywords
- apoptosis, BH3 peptides, Bcl-2 family proteins, Bid, protein-protein interaction, leukemia, xenografts, cell-permeable peptide, death domain
- MeSH terms
- Alkenes, Animals, Bridged-Ring Compounds, Carrier Proteins, Cell Division, Cell Membrane, Dose-Response Relationship, Drug, Humans, Leukemia, Experimental, Mitochondria, Liver, Neoplasm Transplantation, Peptide Fragments, Peptides, Protein Binding, Proto-Oncogene Proteins, Endosomes, Transplantation, Heterologous, Protein Engineering, Mice, SCID, Apoptosis, Leukemic Infiltration, Protein Structure, Secondary, Protein Structure, Tertiary, Molecular Mimicry, Jurkat Cells, Proto-Oncogene Proteins c-bcl-2, Cytochromes c, Cell Line, Tumor, BH3 Interacting Domain Death Agonist Protein, Mice
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