Using an AraC-based three-hybrid system to detect biocatalysts in vivo
- 1 May 2000
- journal article
- research article
- Published by Springer Nature in Nature Biotechnology
- Vol. 18 (5), 544-547
- https://doi.org/10.1038/75414
Abstract
No abstract availableKeywords
This publication has 17 references indexed in Scilit:
- Catalytic Mechanism of Scytalone Dehydratase: Site-Directed Mutagenisis, Kinetic Isotope Effects, and Alternate SubstratesBiochemistry, 1999
- Molecular evolution by staggered extension process (StEP) in vitro recombinationNature Biotechnology, 1998
- 2,3-Dihydro-2,5-dihydroxy-4H-benzopyran-4-one: A Nonphysiological Substrate for Fungal Melanin Biosynthetic EnzymesAnalytical Biochemistry, 1998
- In vivo versus in vitro screening or selection for catalytic activity in enzymes and abzymesMolecular Biotechnology, 1997
- Three-part inventions: intracellular signaling and induced proximityTrends in Biochemical Sciences, 1996
- A three-hybrid system for detecting small ligand–protein receptor interactionsProceedings of the National Academy of Sciences, 1996
- Structural classification of proteins: new superfamiliesCurrent Opinion in Structural Biology, 1996
- DNA shuffling by random fragmentation and reassembly: in vitro recombination for molecular evolution.Proceedings of the National Academy of Sciences, 1994
- Crystal structure of scytalone dehydratase — a disease determinant of the rice pathogen, Magnaporthe griseaStructure, 1994
- Functional domains of the AraC protein.Proceedings of the National Academy of Sciences, 1993