title: Caged glutathione - triggering protein interaction by light.
abstract: Light, GSH, action! Glutathione (GSH) fulfills a universal role as redox factor, scavenger of reactive oxygen species, and as an essential substrate in the conjugation, detoxification, and reduction reactions catalyzed by glutathione S-transferase (GST). A photoactivatable glutathione allows the GSH-GST network to be triggered by light. GST fusion proteins can be assembled in situ at variable density and structures by laser-scanning activation.
authors.affiliation: Institute of Biochemistry, Biocenter, Cluster of Excellence Frankfurt, Goethe University Frankfurt, Frankfurt am Main, Germany.
authors.forename: Volker
authors.initials: V
authors.lastname: Gatterdam
authors.forename: Tatjana
authors.initials: T
authors.lastname: Stoess
authors.forename: Clara
authors.initials: C
authors.lastname: Menge
authors.forename: Alexander
authors.initials: A
authors.lastname: Heckel
authors.forename: Robert
authors.initials: R
authors.lastname: Tampé
mesh_terms: D031541:Fluorescence Resonance Energy Transfer; D005978:Glutathione / Q000737:chemistry / Q000378:metabolism*; D005982:Glutathione Transferase / Q000378:metabolism*; D006801:Humans; D008027:Light; D010084:Oxidation-Reduction
chemical_list: D005982:Glutathione Transferase; D005978:Glutathione