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Janet L. Schottel

Researcher at University of Minnesota

Publications -  62
Citations -  2461

Janet L. Schottel is an academic researcher from University of Minnesota. The author has contributed to research in topics: Streptomyces scabies & Gene. The author has an hindex of 26, co-authored 62 publications receiving 2388 citations. Previous affiliations of Janet L. Schottel include Stanford University & University of Yamanashi.

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Decay of mRNA in Escherichia coli: investigation of the fate of specific segments of transcripts.

TL;DR: Direct evidence was obtained for 3'-to-5' directionality in the decay of the long-lived mRNA encoded by the ompA gene, and no preferential stability was observed for translated versus untranslated mRNA segments.
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The mercuric and organomercurial detoxifying enzymes from a plasmid-bearing strain of Escherichia coli.

TL;DR: Two separate enzymes, which determine resistance to inorganic mercury and organomercurials, have been purified from the plasmid-bearing Escherichia coli strain J53-1(R831), suggesting that the native enzyme is composed of three identical subunits.
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Volatilisation of mercury and organomercurials determined by inducible R-factor systems in enteric bacteria

TL;DR: THE AUTHORS have screened a large number of R plasmid-bearing Escherichia coli and obtained a few that confer resistance to the organomercurials phenylmercuric acetate (PMA) and methylmerCuric chloride (MMA), which are of interest to see if the mercury(ial) resistance of the bacteria in the alimentary canal influences the fate of ingested mercury(ials).
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A DNA cloning system for interspecies gene transfer in antibiotic-producing Streptomyces.

TL;DR: Selectable plasmid vectors that contain a gene encoding resistance to the antibiotic methylenomycin A and that are suitable for the cloning of endonuclease-generated DNA fragments in Streptomyces species have been constructed and characterised.
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A novel variant of the catalytic triad in the Streptomyces scabies esterase.

TL;DR: The crystal structure of a novel esterase from Streptomyces scabies, a causal agent of the potato scab disease, was solved at 2.1 Å resolution and constitutes the first known natural variation of the chymotrypsin-like triad in which a carboxylic acid is replaced by a neutral hydrogen-bond acceptor.