title: Allosteric drugs: thinking outside the active-site box.
abstract: Recently, a class of small molecules that thermally stabilize the tumor suppressor p53 was selected from a small-molecule library. This, and other recent work, demonstrates the feasibility of taking a lead from nature and selecting new classes of drugs that function by allosteric mechanisms.
authors.affiliation: Harvard Institute of Chemistry and Cell Biology, Boston, MA 02115-5731, USA. brian_dedecker@hms.harvard.edu
authors.forename: B S
authors.initials: BS
authors.lastname: DeDecker
mesh_terms: D000494:Allosteric Regulation; D001665:Binding Sites; D006801:Humans; D019001:Nitric Oxide Synthase / Q000378:metabolism; D052247:Nitric Oxide Synthase Type II; D019151:Peptide Library; D015202:Protein Engineering / Q000379:methods; D016159:Tumor Suppressor Protein p53 / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*
chemical_list: D019151:Peptide Library; D016159:Tumor Suppressor Protein p53; C496319:NOS2 protein, human; D019001:Nitric Oxide Synthase; D052247:Nitric Oxide Synthase Type II