Journal articleAuthors : Nakahara, Emi (2023)
Destabilizing domains (DDs) are an attractive strategy allowing for positive post-transcriptional
small molecule-regulatable control of a fusion protein’s abundance. Yet in many instances, the
currently available DDs suffer from higher-than-desirable basal levels of the fusion protein.
Accordingly, we redesigned the E. coli dihydrofolate reductase (ecDHFR) DD by introducing a
library of ~1200 random ecDHFR mutants fused to YFP into CHO cells. Following su...