ArticleJournal of cell science2011
Bax-derived membrane-active peptides act as potent and direct inducers of apoptosis in cancer cells.
Article in Journal of cell science, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
25 citing papers in PubMed, 56 citations in OpenAlex.
- Next-Generation Anticancer Peptides: Engineering, Nanotheranostics and Clinical Translation.Nanotheranostics · 2026Review
- Review
- Article
- The dual interaction of antimicrobial peptides on bacteria and cancer cells; mechanism of action and therapeutic strategies of nanostructures.Microbial cell factories · 2022Review
- Anti-cancer peptide-based therapeutic strategies in solid tumors.Cellular & molecular biology letters · 2022Article
- Controllable membrane remodeling by a modified fragment of the apoptotic protein Bax.Faraday discussions · 2021Article
- Antitumorigenic effect of insect-derived peptide poecilocorisin-1 in human skin cancer cells through regulation of Sp1 transcription factor.Scientific reports · 2021Article
- Homogeneous Oligomers of Pro-apoptotic BAX Reveal Structural Determinants of Mitochondrial Membrane Permeabilization.Molecular cell · 2020Article
- Mechanistic Landscape of Membrane-Permeabilizing Peptides.Chemical reviews · 2019Review
- Evaluation of cell damage induced by irradiated Zinc-Phthalocyanine-gold dendrimeric nanoparticles in a breast cancer cell line.Biomedical journal · 2018Article
- Subcellular Localization and Dynamics of the Bcl-2 Family of Proteins.Frontiers in cell and developmental biology · 2018Review
- Connecting mitochondrial dynamics and life-or-death events via Bcl-2 family proteins.Neurochemistry international · 2017Review
- Evaluation of the use of therapeutic peptides for cancer treatment.Journal of biomedical science · 2017Review
- Systemic Delivery of Tumor-Targeted Bax-Derived Membrane-Active Peptides for the Treatment of Melanoma Tumors in a Humanized SCID Mouse Model.Molecular therapy : the journal of the American Society of Gene Therapy · 2017Article
- Bak apoptotic pores involve a flexible C-terminal region and juxtaposition of the C-terminal transmembrane domains.Cell death and differentiation · 2015Article
- The CT20 peptide causes detachment and death of metastatic breast cancer cells by promoting mitochondrial aggregation and cytoskeletal disruption.Cell death & disease · 2014Article
- Targeting cancer cell mitochondria as a therapeutic approach.Future medicinal chemistry · 2013Review
- Article
- Targeting malignant mitochondria with therapeutic peptides.Therapeutic delivery · 2012Review
- Rational development of a cytotoxic peptide to trigger cell death.Molecular pharmaceutics · 2012Article
Corrections and comments
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Authors and funding
10 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Although many cancer cells are primed for apoptosis, they usually develop resistance to cell death at several levels. Permeabilization of the outer mitochondrial membrane, which is mediated by proapoptotic Bcl-2 family members such as Bax, is considered as a point of no return for initiating apoptotic cell death. This crucial role has placed Bcl-2 family proteins as recurrent targets for anticancer drug development. Here, we propose and demonstrate a new concept based on minimal active versions of Bax to induce cell death independently of endogenous Bcl-2 proteins. We show that membrane-active segments of Bax can directly induce the release of mitochondria-residing apoptogenic factors and commit tumor cells promptly and irreversibly to caspase-dependent apoptosis. On this basis, we designed a peptide encompassing part of the Bax pore-forming domain, which can target mitochondria, induce cytochrome c release and trigger caspase-dependent apoptosis. Moreover, this Bax-derived 'poropeptide' produced effective tumor regression after peritumoral injection in a nude mouse xenograft model. Thus, peptides derived from proteins that form pores in the mitochondrial outer membrane represent novel templates for anticancer agents.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.