Abstract
S100B interacts with the p53 protein in a calcium-dependent manner and down-regulates its function as a tumor suppressor. Therefore, inhibiting the S100B-p53 interaction represents a new approach for restoring functional wild-type p53 in cancers with elevated S100B such as found in malignant melanoma. A discussion of the biological rational for targeting S100B and a description of methodologies relevant to the discovery of compounds that inhibit S100B-p53 binding, including computational techniques, structural biology techniques, and cellular assays, is presented.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
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Review
MeSH terms
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Biomarkers, Tumor
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Calcium / metabolism
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Computer-Aided Design
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Drug Design
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Female
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Humans
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Magnetic Resonance Spectroscopy
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Male
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Molecular Structure
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Nerve Growth Factors / antagonists & inhibitors*
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Nerve Growth Factors / metabolism
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S100 Calcium Binding Protein beta Subunit
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S100 Proteins / antagonists & inhibitors*
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S100 Proteins / metabolism
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Solubility
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Spectrometry, Fluorescence
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Tumor Suppressor Protein p53 / metabolism
Substances
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Biomarkers, Tumor
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Nerve Growth Factors
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S100 Calcium Binding Protein beta Subunit
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S100 Proteins
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S100B protein, human
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Tumor Suppressor Protein p53
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Calcium