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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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An expanding genetic code.

TL;DR: Recent advances that make it possible to add new building blocks systematically to the genetic codes of bacteria, yeast and mammalian cells are described, which will enable the detailed investigation of protein structure and function, which is not possible with conventional mutagenesis.
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Monitoring the conformational fluctuations of DNA hairpins using single-pair fluorescence resonance energy transfer.

TL;DR: The findings indicate that current models should consider sequence dependence in calculating ssDNA thermostability and the surface immobilization chemistries and other experimental techniques described here should prove useful for studies of single-molecule populations and dynamics.
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Redirection of genetically engineered CAR-T cells using bifunctional small molecules.

TL;DR: It is demonstrated that a bifunctional small molecule "switch" consisting of folate conjugated to fluorescein isothiocyanate (folate-FITC) can redirect and regulate FITC-specific CAR-T cell activity toward folate receptor (FR)-overexpressing tumor cells.
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Identification of p53 regulators by genome-wide functional analysis

TL;DR: HES1, HEY1, and TFAP4, and OSR1, which are members of the basic helix-loop-helix transcription family, were shown to activate p53 through repression of HDM2 transcription and to induce apoptosis in vivo, suggesting that these transcription factors areMembers of an evolutionarily conserved network that governs p53 function.
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Recombinant expression of selectively sulfated proteins in Escherichia coli

TL;DR: The selective incorporation of sulfotyrosine into proteins in bacteria is reported by genetically encoding the modified amino acid in response to the amber nonsense codon TAG, and it is shown that this strategy enables direct expression in Escherichia coli of sulfo-hirudin, previously inaccessible through recombinant methods.