Scientific Reports · 2013 · 40 citations · 39 references
Life SciencesMolecular BiologyOncologyCarcinogenesisMolecular OncologyStructural BiologyCancer Molecular PathologyProtein Complex AnalysisProtein StructureProtein TargetingTumor Suppressor GenesAmino AcidsCell Motility ModulationNeuroblastoma BiologyProtein Binding In OncologyProtein Complex CharacterizationProtein Expression LevelsTumor Cell MotilityTumor-targeting Peptides
Nm23-H1 is one of the most interesting candidate genes for a relevant role in Neuroblastoma pathogenesis. H-Prune is the most characterized Nm23-H1 binding partner, and its overexpression has been shown in different human cancers. Our study focuses on the role of the Nm23-H1/h-Prune protein complex in Neuroblastoma. Using NMR spectroscopy, we performed a conformational analysis of the h-Prune C-terminal to identify the amino acids involved in the interaction with Nm23-H1. We developed a competitive permeable peptide (CPP) to impair the formation of the Nm23-H1/h-Prune complex and demonstrated that CPP causes impairment of cell motility, substantial impairment of tumor growth and metastases formation. Meta-analysis performed on three Neuroblastoma cohorts showed Nm23-H1 as the gene highly associated to Neuroblastoma aggressiveness. We also identified two other proteins (PTPRA and TRIM22) with expression levels significantly affected by CPP. These data suggest a new avenue for potential clinical application of CPP in Neuroblastoma treatment.
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Alvaro Leone, Ursula Flatow, C. Richter King et al. · Cell · 1991 · 546 citations · Full text
Medicine, Cancer Biology, Oncology +17
LIN28B induces neuroblastoma and enhances MYCN levels via let-7 suppression
Jan J. Molenaar, Raquel Domingo-Fernandéz, Marli E. Ebus et al. · Nature Genetics · 2012 · 384 citations · Full text
Medicine, Cancer Biology, Oncology +12
The ALKF1174L Mutation Potentiates the Oncogenic Activity of MYCN in Neuroblastoma
Teeara Berry, William Luther, Namrata Bhatnagar et al. · Cancer Cell · 2012 · 327 citations · Full text