P
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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Probing Protein Structure and Function with an Expanded Genetic Code
TL;DR: A general biosynthetic method has been developed which makes it possible to site-specifically incorporate unnatural amino acids with novel properties into proteins, used to study the stability, specificity, and catalytic properties of a number of proteins.
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Auranofin exerts broad-spectrum bactericidal activities by targeting thiol-redox homeostasis
Michael B. Harbut,Catherine Vilchèze,Xiaozhou Luo,Mary E. Hensler,Hui Guo,Baiyuan Yang,Arnab Chatterjee,Victor Nizet,William R. Jacobs,Peter G. Schultz,Feng Wang +10 more
TL;DR: The results suggest that the thioredoxin-mediated redox cascade of Gram-positive pathogens is a valid target for the development of antibacterial drugs, and that the existing clinical agent auranofin may be repurposed to aid in the treatment of several important antibiotic-resistant pathogens.
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A general and efficient route for chemical aminoacylation of transfer RNAs
TL;DR: These protocols greatly simplify the use of chemically misacylated tRNAs in the synthesis of proteins containing unnatural amino acids, as well as in studies of protein biosynthesis.
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An approach to rapid protein crystallization using nanodroplets
Bernard D. Santarsiero,Derek Yegian,Christian C. Lee,Glen Spraggon,J. Gu,D. Scheibe,D. C. Uber,Earl Cornell,Robert Nordmeyer,William F. Kolbe,Jian Jin,Arthur Jones,Joseph M. Jaklevic,Peter G. Schultz,Peter G. Schultz,Raymond C. Stevens,Raymond C. Stevens +16 more
TL;DR: In this article, an approach that enables up to a two order of magnitude reduction in the amount of protein required and a tenfold reduction in time required for vapor-diffusion protein crystallization is reported.
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A new strategy for the site-specific modification of proteins in vivo.
TL;DR: It is demonstrated that proteins containing m-acetyl-l-phenylalanine or p-acetylene-like amino acids can be selectively labeled with hydrazide derivatives not only in vitro but also in living cells.