G
Gordon E. Neal
Researcher at University of Leicester
Publications - 61
Citations - 2913
Gordon E. Neal is an academic researcher from University of Leicester. The author has contributed to research in topics: Aflatoxin & Glutathione. The author has an hindex of 30, co-authored 61 publications receiving 2878 citations. Previous affiliations of Gordon E. Neal include Medical Research Council.
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Journal ArticleDOI
Mechanism of action of dietary chemoprotective agents in rat liver: induction of phase I and II drug metabolizing enzymes and aflatoxin B1 metabolism.
Margaret M. Manson,Helen W.L. Ball,Mandy C. Barrett,Helen L. Clark,David J. Judah,Gary Williamson,Gordon E. Neal +6 more
TL;DR: These studies indicate the relative contributions of phase I and II metabolism in the overall protective effect in rat, and care should be taken that a similar balance is achieved in man, and that relevant enzymes or iso forms are induced.
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Evidence for involvement of multiple forms of cytochrome P-450 in aflatoxin B1 metabolism in human liver.
TL;DR: The finding that antibodies to P450IA2 and P450IIA1 were also effective inhibitors of metabolism in many of the samples demonstrated that, although P450IIIA probably plays an important role in AFB1 activation, several other cytochrome P-450 forms have the capacity to activate the toxin.
Journal Article
Chemoprevention of aflatoxin B1 hepatocarcinogenesis by coumarin, a natural benzopyrone that is a potent inducer of aflatoxin B1-aldehyde reductase, the glutathione S-transferase A5 and P1 subunits, and NAD(P)H:quinone oxidoreductase in rat liver
Vincent P. Kelly,Elizabeth M. Ellis,Margaret M. Manson,Simon A. Chanas,Graeme J. Moffat,Ronald McLeod,David J. Judah,Gordon E. Neal,John D. Hayes +8 more
TL;DR: The data suggest that consumption of a CMRN-containing diet provides substantial protection against the initiation of AFB1 hepatocarcinogenesis in the rat, and the ability of the benzopyrone to inhibit either AFB1-initiated preneoplastic nodules or AFB1- initiated liver tumors was investigated.
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Contribution of the glutathione S-transferases to the mechanisms of resistance to aflatoxin B1.
TL;DR: Circumstantial evidence exists that amongst these mechanisms the glutathione S-transferases, through their ability to detoxify AFB1-8,9-epoxide, play a major role in determining the sensitivity of cells to AFB1.
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Molecular cloning and heterologous expression of a cDNA encoding a mouse glutathione S-transferase Yc subunit possessing high catalytic activity for aflatoxin B1-8,9-epoxide.
TL;DR: Comparison of the deduced amino acid sequence of the mouse Yc polypeptide with the primary structures of the rat Alpha-class GST enzymes revealed that it is more closely related to the ethoxyquin-induced rat liver Yc2 subunit than to the constitutively expressed rat Liver GST Yc1 subunit.