ArticleInternational journal of high throughput screening2010
In vitro screening and structural characterization of inhibitors of the S100B-p53 interaction.
Article in International journal of high throughput screening, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
20 citing papers in PubMed, 30 citations in OpenAlex.
- Roles of the Receptor for Advanced Glycation End Products and Its Ligands in the Pathogenesis of Alzheimer's Disease.International journal of molecular sciences · 2025Review
- A Structural Perspective on Calprotectin as a Ligand of Receptors Mediating Inflammation and Potential Drug Target.Biomolecules · 2022Review
- Bacteriophage PRD1 as a nanoscaffold for drug loading.Nanoscale · 2021Article
- Targeting S100 Calcium-Binding Proteins with Small Molecule Inhibitors.Methods in molecular biology (Clifton, N.J.) · 2019Article
- S100 proteins as therapeutic targets.Biophysical reviews · 2018Review
- Structural Basis for S100B Interaction with its Target Proteins.Journal of molecular and genetic medicine : an international journal of biomedical research · 2018Article
- The Activation of Protein Kinase A by the Calcium-Binding Protein S100A1 Is Independent of Cyclic AMP.Biochemistry · 2017Article
- Novel protein-inhibitor interactions in site 3 of Ca(2+)-bound S100B as discovered by X-ray crystallography.Acta crystallographica. Section D, Structural biology · 2016Article
- Fluorescence polarization assays in high-throughput screening and drug discovery: a review.Methods and applications in fluorescence · 2016Article
- Small Molecule Inhibitors of Ca(2+)-S100B Reveal Two Protein Conformations.Journal of medicinal chemistry · 2016Article
- Structural insights into xenobiotic and inhibitor binding to human aldehyde oxidase.Nature chemical biology · 2015Article
- Covalent small molecule inhibitors of Ca(2+)-bound S100B.Biochemistry · 2014Article
- A fluorescent carbapenem for structure function studies of penicillin-binding proteins, β-lactamases, and β-lactam sensors.Analytical biochemistry · 2014Article
- Functions of S100 proteins.Current molecular medicine · 2013Review
- In vivo screening of S100B inhibitors for melanoma therapy.Methods in molecular biology (Clifton, N.J.) · 2013Article
- The evolution of S100B inhibitors for the treatment of malignant melanoma.Future medicinal chemistry · 2013Review
- Target binding to S100B reduces dynamic properties and increases Ca(2+)-binding affinity for wild type and EF-hand mutant proteins.Journal of molecular biology · 2012Article
- S100 proteins as diagnostic and prognostic markers in colorectal and hepatocellular carcinoma.Hepatitis monthly · 2012Article
- Molecular dynamic simulation insights into the normal state and restoration of p53 function.International journal of molecular sciences · 2012Review
- The Calcium-Dependent Interaction of S100B with Its Protein Targets.Cardiovascular psychiatry and neurology · 2010Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
10 authors at 1 institution in 1 country.
Funding
Abstract
S100B is highly over-expressed in many cancers, including malignant melanoma. In such cancers, S100B binds wild-type p53 in a calcium-dependent manner, sequestering it, and promoting its degradation, resulting in the loss of p53-dependent tumor suppression activities. Therefore, S100B inhibitors may be able to restore wild-type p53 levels in certain cancers and provide a useful therapeutic strategy. In this regard, an automated and sensitive fluorescence polarization competition assay (FPCA) was developed and optimized to screen rapidly for lead compounds that bind Ca(2+)-loaded S100B and inhibit S100B target complex formation. A screen of 2000 compounds led to the identification of 26 putative S100B low molecular weight inhibitors. The binding of these small molecules to S100B was confirmed by nuclear magnetic resonance spectroscopy, and additional structural information was provided by x-ray crystal structures of several compounds in complexes with S100B. Notably, many of the identified inhibitors function by chemically modifying Cys84 in protein. These results validate the use of high-throughput FPCA to facilitate the identification of compounds that inhibit S100B. These lead compounds will be the subject of future optimization studies with the ultimate goal of developing a drug with therapeutic activity for the treatment of malignant melanoma and/or other cancers with elevated S100B.
Identifiers
What OpenQuestion holds
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.