R
Richard A. Lerner
Researcher at Scripps Research Institute
Publications - 664
Citations - 55701
Richard A. Lerner is an academic researcher from Scripps Research Institute. The author has contributed to research in topics: Catalysis & Antibody. The author has an hindex of 107, co-authored 661 publications receiving 53678 citations. Previous affiliations of Richard A. Lerner include University of California, Irvine & ShanghaiTech University.
Papers
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Journal ArticleDOI
Proline-Catalyzed Direct Asymmetric Aldol Reactions
TL;DR: The finding that the amino acid proline is an effective asymmetric catalyst for the direct aldol reaction between unmodified acetone and a variety of aldehydes is reported.
Journal ArticleDOI
Molecular characterization of an enzyme that degrades neuromodulatory fatty-acid amides
Benjamin F. Cravatt,Dan K. Giang,Stephen P. Mayfield,Dale L. Boger,Richard A. Lerner,Norton B. Gilula +5 more
TL;DR: It is shown that oleamide hydrolase may serve as the general inactivating enzyme for a growing family of bioactive signalling molecules, the fatty-acid amides6–8, and the structure and sleep-inducing properties of cis-9-octadecenamide, a lipid isolated from the cerebrospinal fluid of sleep-deprived cats are reported.
Journal ArticleDOI
Generation of a large combinatorial library of the immunoglobulin repertoire in phage lambda
William D. Huse,Lakshmi Sastry,Sheila A. Iverson,Angray S. Kang,Angray S. Kang,Michelle A. Alting-Mees,Dennis R. Burton,Dennis R. Burton,Stephen J. Benkovic,Stephen J. Benkovic,Richard A. Lerner +10 more
TL;DR: A novel bacteriophage lambda vector system was used to express in Escherichia coli a combinatorial library of Fab fragments of the mouse antibody repertoire, which allows rapid and easy identification of monoclonal Fab fragments in a form suitable for genetic manipulation.
Journal ArticleDOI
Assembly of combinatorial antibody libraries on phage surfaces: the gene III site.
TL;DR: A phagemid system was developed for the monovalent display of combinatorial antibody Fab libraries on the surface of filamentous phage M13, and may replace current antibody cloning techniques.
Patent
Heterodimeric receptor libraries using phagemids
TL;DR: In this article, a filamentous phage comprising a matrix of cpVIII proteins encapsulating a genome encoding first and second polypeptides of an antogenously assembling receptor, such as an antibody, is presented.