title: Protein and Protease Sensing by Allosteric Derepression.
abstract: Peptide motifs are crucial mediators of protein-protein interactions as well as sites of specific protease activity. The detection and characterization of these events is therefore indispensable for a detailed understanding of cellular regulation. Here, we present versatile and modular sensors that allow the user to detect protease activity and protein-peptide interactions, as well as to screen for inhibitors using chromogenic, fluorescent, or luminescent output.
authors.affiliation: p53 Laboratory, A*STAR Agency for Science, Technology and Research, #06-04/05 Neuros, 138648, Singapore, Singapore.
authors.forename: Hui Chin
authors.initials: HC
authors.lastname: Goh
authors.affiliation: p53 Laboratory, A*STAR Agency for Science, Technology and Research, #06-04/05 Neuros, 138648, Singapore, Singapore. fghadessy@p53Lab.a-star.edu.sg.
authors.forename: Farid J
authors.initials: FJ
authors.lastname: Ghadessy
authors.affiliation: p53 Laboratory, A*STAR Agency for Science, Technology and Research, #06-04/05 Neuros, 138648, Singapore, Singapore.
authors.forename: Saurabh
authors.initials: S
authors.lastname: Nirantar
mesh_terms: D000494:Allosteric Regulation / Q000235:genetics*; D001483:Base Sequence; D015374:Biosensing Techniques / Q000379:methods; D010447:Peptide Hydrolases / Q000235:genetics*; D010455:Peptides / Q000235:genetics*; D054730:Protein Interaction Domains and Motifs / Q000235:genetics
chemical_list: D010455:Peptides; D010447:Peptide Hydrolases
keywords: Drug screening; Protease sensors; Protein-protein interaction