Bookedited by Gerard Drews and Marcus Bantscheff.
Contents:
Mass spectrometry-based chemoproteomic approaches
Chemical proteomics in drug discovery
Compound immobilization and drug-affinity chromatography
Affinity-based chemoproteomics with small molecule-peptide conjugates
A chemical proteomic probe for detecting dehydrogenases: Catechol rhodanine
Probing proteomes with benzophenone photoprobes
Biotinylated probes for the analysis of protein modification by electrophiles
Profiling of methyltransferases and other S-adenosyl-l: -homocysteine-binding proteins by capture compound mass spectrometry
Identifying cellular targets of small-molecule probes and drugs with biochemical enrichment and SILAC
Determination of kinase inhibitor potencies in cell extracts by competition binding assays and isobaric mass tags
Affinity-based profiling of dehydrogenase subproteomes
Probing the specificity of protein-protein interactions by quantitative chemical proteomics
Fluorescence-based proteasome activity profiling
Chemical cross-linking and high-resolution mass spectrometry to study protein-drug interactions
Monitoring ligand modulation of protein-protein interactions by chemical cross-linking and high-mass MALDI mass spectrometry
Time-controlled transcardiac perfusion crosslinking for in vivo interactome studies
Ligand discovery using small-molecule microarrays
Working with small molecules : preparing and storing stock solutions and determination of kinetic solubility
A database for chemical proteomics : ChEBI
Working with small molecules: Rules-of-thumb of Drug likeness.