ArticleInternational journal of nanomedicine2014
A nanotechnological, molecular-modeling, and immunological approach to study the interaction of the anti-tumorigenic peptide p28 with the p53 family of proteins.
Article in International journal of nanomedicine, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 18 citations in OpenAlex.
- A multi-targeted therapeutic strategy for triple-negative breast cancer: the tumor-targeting peptide p28 enhances chemotherapy, induces apoptosis, crosses the blood-brain barrier, and suppresses metastasis.Apoptosis : an international journal on programmed cell death · 2026Article
- Automated assembly of molecular mechanisms at scale from text mining and curated databases.Molecular systems biology · 2023Article
- Review
- Review
- Toward Cancer Diagnostics of the Tumor Suppressor p53 by Surface Enhanced Raman Spectroscopy.Sensors (Basel, Switzerland) · 2020Review
- p28 Bacterial Peptide, as an Anticancer Agent.Frontiers in oncology · 2020Review
- The Effect of Bacterial Peptide p28 on Viability and Apoptosis Status of P53-null HeLa Cells.Advanced pharmaceutical bulletin · 2019Article
- Bacterial cupredoxin azurin hijacks cellular signaling networks: Protein-protein interactions and cancer therapy.Protein science : a publication of the Protein Society · 2017Review
- Surface Plasmon Resonance Sensing of Biorecognition Interactions within the Tumor Suppressor p53 Network.Sensors (Basel, Switzerland) · 2017Review
- High Expression of Pirh2 is Associated with Poor Prognosis in Glioma.Cellular and molecular neurobiology · 2017Article
- MDM2-MDM4 molecular interaction investigated by atomic force spectroscopy and surface plasmon resonance.International journal of nanomedicineArticle
Corrections and comments
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Authors and funding
5 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
p28 is an anionic, amphipathic, cell-penetrating peptide derived from the cupredoxin azurin that binds to the DNA-binding domain (DBD) of the tumor suppressor protein, p53, and induces a post-translational increase in the level of wild type and mutated p53 in a wide variety of human cancer cells. As p63 and p73, additional members of the p53 superfamily of proteins, also appear to be involved in the cellular response to cancer therapy and are reportedly required for p53-induced apoptosis, we asked whether p28 also binds to p63 and p73. Atomic force spectroscopy demonstrates that p28 forms a stable, high-affinity complex with full-length p63, the DBD of p63, and full-length p73. Exposure to p28 decreased the level of TAp63α and ΔNp63α, the truncated form of p63, in p53 wild type and mutated human breast cancer cells, respectively. p28 increased the level of TAp73α, but not ΔNp73α, in the same breast cancer cell lines. In contrast, p28 increased the level of the TA and ΔN isoforms of p63 in p53 wild type, but not in p53 mutated melanoma cells, while decreasing TA p73α in p53 wild type and mutated human melanoma cells. All changes were mirrored by an associated change in the expression of the HECT E3 ligases Itch/AIP4, AIP5, and the RING E3 ligase Pirh2, but not in the receptor for activated C kinase or the RING E3 ligases Mdm2 and Cop1. Collectively, the data suggest that molecules such as p28 bind with high affinity to the DBD of p63 and p73 and alter their expression independent of the Mdm2 and Cop1 pathways.
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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.