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John E. Linz

Researcher at Michigan State University

Publications -  110
Citations -  6109

John E. Linz is an academic researcher from Michigan State University. The author has contributed to research in topics: Aspergillus parasiticus & Aflatoxin. The author has an hindex of 43, co-authored 110 publications receiving 5762 citations. Previous affiliations of John E. Linz include Louisiana State University & United States Department of Agriculture.

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Clustered pathway genes in aflatoxin biosynthesis.

TL;DR: Aflatoxins, a group of polyketide-derived furanocoumarins, are the most toxic and carcinogenic compounds among the known mycotoxins and there are only four major aflatoxINS, B1, B2, G1, and G2.
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Comparative mapping of aflatoxin pathway gene clusters in Aspergillus parasiticus and Aspergillus flavus.

TL;DR: The physical distances (in kilobase pairs) and the directions of transcription of these genes have been determined for both aflatoxigenic species and the order is related to the order in enzymatic steps required for aflatoxin biosynthesis.
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Cloning of the Aspergillus parasiticus apa-2 gene associated with the regulation of aflatoxin biosynthesis.

TL;DR: An Aspergillus parasiticus gene, designated apa-2, was identified as a regulatory gene associated with aflatoxin biosynthesis and was found to complement an A. flavus afl-2 mutant strain for a flatoxin production, suggesting that apA-2 is functionally homologous to aFL-2.
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A key role for vesicles in fungal secondary metabolism

TL;DR: A unique 2-branch model is proposed to illustrate the proposed role for VeA in regulation of aflatoxisome development and aflatoxin gene expression, which is at least in part mediated by Velvet, a global regulator of Aspergillus secondary metabolism.
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Isolation and characterization of a gene from Aspergillus parasiticus associated with the conversion of versicolorin A to sterigmatocystin in aflatoxin biosynthesis.

TL;DR: DNA isolated from the wild-type aflatoxin-producing fungus Aspergillus parasiticus NRRL 5862 was used to construct a cosmid genomic DNA library employing the homologous gene (pyrG) encoding orotidine monophosphate decarboxylase for selection of fungal transformants, revealing striking similarity with Streptomyces ketoreductases involved in polyketide biosynthesis.