ArticleInternational journal of nanomedicine2018
Imaging and kinetics of the bimolecular complex formed by the tumor suppressor p53 with ubiquitin ligase COP1 as studied by atomic force microscopy and surface plasmon resonance.
Article in International journal of nanomedicine, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Possible Applications of Azurin, a Copper-Containing Protein, in Cancer Treatment: Prospects and Challenges.Current drug targets · 2026Review
- Interaction between miR4749 and Human Serum Albumin as Revealed by Fluorescence, FRET, Atomic Force Spectroscopy and Computational Modelling.International journal of molecular sciences · 2022Article
- Direct Interaction of miRNA and circRNA with the Oncosuppressor p53: An Intriguing Perspective in Cancer Research.Cancers · 2021Review
- Toward Cancer Diagnostics of the Tumor Suppressor p53 by Surface Enhanced Raman Spectroscopy.Sensors (Basel, Switzerland) · 2020Review
- Regulating tumor suppressor genes: post-translational modifications.Signal transduction and targeted therapy · 2020Review
- Anticancer Actions of Azurin and Its Derived Peptide p28.The protein journal · 2020Review
- Isothermal titration calorimetry and surface plasmon resonance analysis using the dynamic approach.Biochemistry and biophysics reports · 2020Article
- p28 Bacterial Peptide, as an Anticancer Agent.Frontiers in oncology · 2020Review
- Interaction of human hemoglobin and semi-hemoglobins with the Staphylococcus aureus hemophore IsdB: a kinetic and mechanistic insight.Scientific reports · 2019Article
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Authors and funding
3 authors.
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Abstract
p53 plays an important role in the safeguard of the genome but it is frequently downregulated mainly by E3 ubiquitin ligases among which COP1 plays an important role. The overexpression of COP1 has been reported to occur in several tumors and may be indicative of its overall oncogenic effect, which in turn might be originated by a direct interaction of COP1 with p53. Such an interaction may constitute a rewarding target for anticancer drug design strategies; therefore, a deeper understanding of its underlying molecular mechanism and kinetics is needed. The formation of a single p53-COP1 bimolecular complex was visualized by atomic force microscopy imaging on a mica substrate. The kinetic characterization of the complex, performed by atomic force spectroscopy and surface plasmon resonance, provided a
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