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- W2165422969 endingPage "493" @default.
- W2165422969 startingPage "461" @default.
- W2165422969 abstract "Ten years have passed since the initial reports that antibodies could be programmed to have enzymatic activity by immunization with a transition-site analog. Much of the research over the last decade has focused on defining the scope and generality of antibody catalysis; however, during the past two years the first few crystal structures of catalytic antibody transition-state analogs have been reported. This review analyzes four such structures of catalytic antibodies that catalyze markedly different reactions, including ester hydrolysis, sulfide oxidation, and a pericyclic rearrangement. Structure-function relations for these catalysts are discussed and compared to the structure and function of natural enzymes, as well as the chemistry that occurs in solution." @default.
- W2165422969 created "2016-06-24" @default.
- W2165422969 creator A5017706607 @default.
- W2165422969 creator A5025029436 @default.
- W2165422969 date "1997-06-01" @default.
- W2165422969 modified "2023-09-24" @default.
- W2165422969 title "THE STRUCTURAL AND FUNCTIONAL BASIS OF ANTIBODY CATALYSIS" @default.
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