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Jean-Luc Pernodet

Researcher at Université Paris-Saclay

Publications -  97
Citations -  4922

Jean-Luc Pernodet is an academic researcher from Université Paris-Saclay. The author has contributed to research in topics: Gene & Streptomyces. The author has an hindex of 37, co-authored 95 publications receiving 4250 citations. Previous affiliations of Jean-Luc Pernodet include Institut Gustave Roussy & Aventis Pharma.

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Minimum Information about a Biosynthetic Gene cluster.

Marnix H. Medema, +164 more
TL;DR: This work proposes the Minimum Information about a Biosynthetic Gene cluster (MIBiG) data standard, to facilitate consistent and systematic deposition and retrieval of data on biosynthetic gene clusters.
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Recombinant Environmental Libraries Provide Access to Microbial Diversity for Drug Discovery from Natural Products

TL;DR: The data reinforce the idea that exploiting previously unknown or uncultivated microorganisms for the discovery of novel natural products has potential value and suggest a strategy for developing this technology into a realistic and effective drug discovery tool.
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Towards the sustainable discovery and development of new antibiotics

TL;DR: In this paper, the authors present a strategic blueprint to substantially improve our ability to discover and develop new antibiotics, and propose both short-term and long-term solutions to overcome the most urgent limitations in the various sectors of research and funding.
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Antibiotic resistance gene cassettes derived from the omega interposon for use in E. coli and Streptomyces.

TL;DR: Three antibiotic resistance gene cassettes, derived from the omega interposon, were constructed, carrying different antibiotic resistance genes, conferring resistance to geneticin, hygromycin or viomycin, flanked by short inverted repeats containing transcription and translation termination signals and synthetic polylinkers.
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Cyclodipeptide synthases are a family of tRNA-dependent peptide bond–forming enzymes

TL;DR: It is demonstrated that AlbC and several other bacterial proteins, presenting moderate similarity to AlbC, also use aminoacyl-tRNAs as substrates to catalyze the formation of the DKP peptide bonds and belong to a newly defined family of enzymes that are named cyclodipeptide synthases (CDPSs).