title: Prevention of Serpin Misfolding by RNA Aptamers.
abstract: Owing to their structural flexibility, most serpins inhibit the cognate proteases in a fast and specific manner and also are susceptible to pathogenic misfolding. In this issue of Cell Chemical Biology, Madsen et al. (2016) report on the selection and characterization of an RNA aptamer that stabilizes α1-antichymotrypsin L55P mutant without interfering with the protease inhibitory activity.
authors.affiliation: Laboratory for Therapeutic and Diagnostic Antibodies, Department of Pharmaceutical and Pharmacological Sciences, KU Leuven, 3000 Leuven, Belgium.
authors.forename: Xiaohua
authors.initials: X
authors.lastname: Zhou
authors.affiliation: Laboratory for Therapeutic and Diagnostic Antibodies, Department of Pharmaceutical and Pharmacological Sciences, KU Leuven, 3000 Leuven, Belgium. Electronic address: paul.declerck@kuleuven.be.
authors.forename: Paul J
authors.initials: PJ
authors.lastname: Declerck
mesh_terms: D000595:Amino Acid Sequence; D052157:Aptamers, Nucleotide; D009154:Mutation; D012313:RNA; D015843:Serpins / Q000235:genetics*
chemical_list: D052157:Aptamers, Nucleotide; D015843:Serpins; D012313:RNA