P
Pius Joseph
Researcher at National Institute for Occupational Safety and Health
Publications - 51
Citations - 3946
Pius Joseph is an academic researcher from National Institute for Occupational Safety and Health. The author has contributed to research in topics: Gene expression & Toxicity. The author has an hindex of 25, co-authored 48 publications receiving 3723 citations. Previous affiliations of Pius Joseph include University of South Florida & National Institutes of Health.
Papers
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Journal ArticleDOI
Molecular and cellular mechanisms of cadmium carcinogenesis
TL;DR: It becomes clear that there exist multiple mechanisms which contribute to the carcinogenicity of cadmium, although the relative weights of these contributions are difficult to estimate.
Journal ArticleDOI
Mechanisms of cadmium carcinogenesis.
TL;DR: The available evidence indicates that oxidative stress plays a central role in Cd carcinogenesis because of its involvement in C d-induced aberrant gene expression, inhibition of DNA damage repair, and inhibition of apoptosis.
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Disruption of the DT diaphorase (NQO1) gene in mice leads to increased menadione toxicity.
Venugopal Radjendirane,Pius Joseph,Ying Hue Lee,Shioko Kimura,Andres J. Klein-Szanto,Frank J. Gonzalez,Anil K. Jaiswal +6 more
TL;DR: In this paper, a NQO1-null mouse was produced using targeted gene disruption and showed increased toxicity when administered menadione compared with wild-type mice, which can be used to determine the role of this enzyme in sensitivity to toxicity and carcinogenesis.
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NAD(P)H:quinone oxidoreductase1 (DT diaphorase) specifically prevents the formation of benzo[a]pyrene quinone-DNA adducts generated by cytochrome P4501A1 and P450 reductase
Pius Joseph,Anil K. Jaiswal +1 more
TL;DR: Results show that semiquinones can directly bind to DNA and demonstrate that NQO1 activity can specifically reduce the binding of quinone metabolites of BP generated by CYP1A1 and P450 reductase toDNA and protein.
Journal ArticleDOI
Abnormal Microsomal Detoxification Implicated in Fanconi Anemia Group C by Interaction of the FAC Protein With NADPH Cytochrome P450 Reductase
Frank A.E. Kruyt,Taizo Hoshino,Taizo Hoshino,Johnson M. Liu,Johnson M. Liu,Pius Joseph,Pius Joseph,Anil K. Jaiswal,Anil K. Jaiswal,Hagop Youssoufian,Hagop Youssoufian +10 more
TL;DR: FAC binds to NADPH cytochrome-P450 reductase (RED), a microsomal membrane protein involved in electron transfer, in both transfected COS-1 and normal murine liver cells, and is proposed to play a fundamental role in vivo by attenuating the activity of RED, thereby regulating a major detoxification pathway in mammalian cells.