Document Detail

Identification of small molecules affecting p53-MDM2/MDMX interaction by fluorescence polarization.
MedLine Citation:
PMID:  23150440     Owner:  NLM     Status:  MEDLINE    
Fluorescence polarization (FP) has become a powerful technique to quantitatively analyze the binding of a small soluble fluorescence-labeled probe to a larger soluble protein and its displacement by other molecules. Here, we describe a detailed protocol to identify small molecules capable of targeting p53-MDM2/MDMX interactions using a fluorescence polarization assay with Rhodamine-labeled p53 peptides.
Qi Zhang; Hua Lu
Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Methods in molecular biology (Clifton, N.J.)     Volume:  962     ISSN:  1940-6029     ISO Abbreviation:  Methods Mol. Biol.     Publication Date:  2013  
Date Detail:
Created Date:  2012-11-15     Completed Date:  2013-04-29     Revised Date:  2013-09-09    
Medline Journal Info:
Nlm Unique ID:  9214969     Medline TA:  Methods Mol Biol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  95-111     Citation Subset:  IM    
Department of Biochemistry & Molecular Biology and Tulane Cancer Center, Tulane University School of Medicine, New Orleans, LA, USA.
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MeSH Terms
Fluorescence Polarization / methods*
Gene Expression
Nuclear Proteins / chemistry*,  genetics
Protein Binding
Proto-Oncogene Proteins / chemistry*,  genetics
Proto-Oncogene Proteins c-mdm2 / chemistry*,  genetics
Reproducibility of Results
Tumor Suppressor Protein p53 / chemistry*,  genetics
Grant Support
Reg. No./Substance:
0/MDM4 protein, human; 0/Nuclear Proteins; 0/Proto-Oncogene Proteins; 0/Tumor Suppressor Protein p53; EC protein, human; EC Proteins c-mdm2

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