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Gordon V. Louie

Researcher at Salk Institute for Biological Studies

Publications -  24
Citations -  1831

Gordon V. Louie is an academic researcher from Salk Institute for Biological Studies. The author has contributed to research in topics: Lyase & Chalcone. The author has an hindex of 16, co-authored 23 publications receiving 1576 citations. Previous affiliations of Gordon V. Louie include Torrey Pines Institute for Molecular Studies & Howard Hughes Medical Institute.

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Architectures, mechanisms and molecular evolution of natural product methyltransferases

TL;DR: It is shown how a widespread protein fold evolved to accommodate chemically diverse methyl acceptors and to catalyse disparate mechanisms suited to the physiochemical properties of the target substrates, suggesting that NPMTs may serve as starting points for generating new biocatalysts.
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Evolution of the chalcone-isomerase fold from fatty-acid binding to stereospecific catalysis

TL;DR: In this article, the crystal structures, ligand-binding properties and in vivo function of several catalytically inactive members of the chalcone isomerase family were reported.
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Genetically encoding unnatural amino acids for cellular and neuronal studies

TL;DR: New strategies for generating orthogonal tRNA-synthetase pairs were presented, which made possible the genetic encoding of diverse unnatural amino acids in different mammalian cells and primary neurons and found that the bulkiness of residues in the inactivation peptide is essential for fast channel inactivation, a finding that had not been possible using conventional mutagenesis.
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Functional analyses of caffeic acid O-methyltransferase and cinnamoyl-CoA-reductase genes from perennial ryegrass (Lolium perenne).

TL;DR: The authors show enhanced digestibility of cinnamoyl CoA-reductase and caffeic acid O-methyltransferase-deficient perennial ryegrass plants grown under glasshouse and field conditions, indicating that both of these lignin biosynthetic genes are promising targets for transgenic approaches aiming to enhance forage quality and improve feedstock plants for biofuel production.
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Discovery of Two Cyanobacterial Phenylalanine Ammonia Lyases: Kinetic and Structural Characterization.

TL;DR: Two cyanobacterial PALs from cyanobacteria, in particular, Anabaena variabilis ATCC 29413 and Nostoc punctiforme ATCC 29133 are identified by screening the genome sequences of these organisms for members of the aromatic amino acid ammonia lyase family.