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Peter G. Schultz

Researcher at Scripps Research Institute

Publications -  901
Citations -  96321

Peter G. Schultz is an academic researcher from Scripps Research Institute. The author has contributed to research in topics: Amino acid & Transfer RNA. The author has an hindex of 156, co-authored 893 publications receiving 89716 citations. Previous affiliations of Peter G. Schultz include Novartis Foundation & University of California, Berkeley.

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A Versatile Platform for Single- and Multiple-Unnatural Amino Acid Mutagenesis in Escherichia coli

TL;DR: A new, highly efficient suppressor plasmid, pUltra, harboring a single copy each of the tRNA and aaRS expression cassettes that exhibits higher suppression activity than its predecessors is described, able to efficiently incorporate up to three UAAs within the same protein at levels up to 30% of the level of wild-type protein expression.
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A genetically encoded fluorescent amino acid.

TL;DR: The fluorescent amino acid l-(7-hydroxycoumarin-4-yl) ethylglycine 1 has been genetically encoded in E. coli in response to the amber TAG codon and should provide a useful probe of protein localization and trafficking, protein conformation changes, and protein-protein interactions.
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A genetically encoded photocaged amino acid

TL;DR: Using a novel genetic selection, a series of synthetase mutants are identified that selectively charge the amber suppresor tRNA with the C8 amino acid, alpha-aminocaprylic acid, and the photocaged amino acids, o-nitrobenzyl cysteine, allowing them to be inserted into proteins in yeast in response to the amber nonsense codon, TAG.
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A chemical biology approach reveals period shortening of the mammalian circadian clock by specific inhibition of GSK-3β

TL;DR: The development of a high-throughput circadian functional assay system that consists of luminescent reporter cells, screening automation, and a data analysis pipeline is reported, finding that small molecule inhibitors of glycogen synthase kinase 3 (GSK-3) consistently caused a strong short period phenotype in contrast to the well-known period lengthening by lithium.
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Mechanistic Studies of the Oxidation of Isoniazid by the Catalase Peroxidase from Mycobacterium tuberculosis

TL;DR: The results suggest that isoniazid is oxidized by the catalase-peroxidase to a reactive species that may act by inactivating an essential enzyme of M. tuberculosis.