C
Christopher T. Walsh
Researcher at Stanford University
Publications - 841
Citations - 79830
Christopher T. Walsh is an academic researcher from Stanford University. The author has contributed to research in topics: Nonribosomal peptide & Active site. The author has an hindex of 139, co-authored 819 publications receiving 74314 citations. Previous affiliations of Christopher T. Walsh include Florida State University & Massachusetts Institute of Technology.
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NMR studies of [U-13C]cyclosporin A bound to human cyclophilin B.
TL;DR: The conformation and active site environment of CsA when bound to CyPA and CyPB are nearly identical as judged by the similarity of the NMR data.
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Inhibitors of sterol biosynthesis as Staphylococcus aureus antibiotics.
TL;DR: A team of investigators that includes structural biologists, chemists, and microbiologists have recently discovered that inhibition of the S. aureus dehydrosqualene synthase reduces bacterial survival during infections, offering a proof-of-principle for such a virulence-targeted approach.
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Kinetic isotope effect analysis of the reaction catalyzed by Trypanosoma congolense trypanothione reductase.
TL;DR: The pH dependence of the kinetic parameters V, V/K for NADH, and V/k for oxidized trypanothione has been determined for trypanothsione reductase from Trypanosoma congolense, and variable magnitudes of the primary deuterium kinetic isotope effects on pyridine nucleotide oxidation are observed on V andV/K when different pyrazine nucleotide substrates are used.
ComponentDOI
The external thioesterase of the Surfactin-Synthetase
Alexander Koglin,Frank Löhr,Frank Bernhard,Vladimir V. Rogov,Dominique P. Frueh,Eric R. Strieter,Mohammad Reza Mofid,Peter Guentert,Gerhard Wagner,Christopher T. Walsh,Mohamed A. Marahiel,Volker Doetsch +11 more
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Covalent CouN7 enzyme intermediate for acyl group shuttling in aminocoumarin biosynthesis.
TL;DR: The last stages of assembly of the aminocoumarin antibiotics, clorobiocin and coumermycin A(1), which target the GyrB subunits of bacterial DNA gyrase, involve enzymatic transfer of the pyrrolyl-2-carbonyl acyl group from a carrier protein to the 3'-OH of the noviosyl moiety of the antibiotic scaffold.