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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 General Strategy for Engineering Noncanonical Amino Acid Dependent Bacterial Growth

TL;DR: Using a tem-perature sensitive selection system, an Escherich-ia coli sliding clamp variant with an orthogonal pro-tein-protein interface is evolved, which contains a Leu273 to p-benzoylphenyl alanine (pBzF) mutation.
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Noncoded Amino Acid Replacement Probes of the Aspartate Aminotransferase Mechanism

TL;DR: This mutant enzyme exhibits kCat/values that are near to those of wild type enzyme; however, the kcat/vs pH profile is much sharper with similar pKas of approximately 7.5 for both the ascending and descending limbs.
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A Strategy for Creating Organisms Dependent on Noncanonical Amino Acids.

TL;DR: This work has devised a barnase-based conditional suicide switch to further lower the escape frequency of the host cells and offers a number of attractive features for controlling host viability, including a single small-molecule-based kill switch, low escape frequency, and unaffected protein function.
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Rational design of antibody protease inhibitors.

TL;DR: This work has generated antibodies that inhibit bovine trypsin and human neutrophil elastase (HNE) with low nanomolar affinities and a highly selective humanized anti-HNE antibody with sub-nanomolar affinity.
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Dorsomorphin promotes human embryonic stem cell self-renewal

TL;DR: The identification of a small molecule that promotes long-term hESC self-renewal is reported, an inhibitor of bone morphogenic protein (BMP) type I receptors (ALK2, ALK3, and ALK6), which maintained the highest percentage of OCT4 positive cells in a dose-dependent manner.