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Natalia V. Dolgova

Researcher at University of Saskatchewan

Publications -  29
Citations -  370

Natalia V. Dolgova is an academic researcher from University of Saskatchewan. The author has contributed to research in topics: Selenium & Arsenite. The author has an hindex of 9, co-authored 27 publications receiving 230 citations. Previous affiliations of Natalia V. Dolgova include Florida State University College of Arts and Sciences & Moscow State University.

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The metal chaperone Atox1 regulates the activity of the human copper transporter ATP7B by modulating domain dynamics

TL;DR: A regulatory mechanism in which Atox1-mediated copper transfer activates ATP7B by releasing inhibitory constraints through increased freedom of MBD1–3 motions is suggested.
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Rethinking the Minamata Tragedy: What Mercury Species Was Really Responsible?

TL;DR: Using newly-available methods to re-examine the cerebellum of historic Cat 717, synchrotron high energy resolution fluorescence detection-X-ray absorption spectroscopy revealed sulfur-bound organometallic mercury with a minor β-HgS phase in factory effluent.
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Distribution of selenium in zebrafish larvae after exposure to organic and inorganic selenium forms

TL;DR: It is found that the organic forms of selenium tested show considerably more toxicity than inorganic forms (selenite and selenate), and that this appears to be correlated with the level of bioaccumulation.
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Dynamics of the metal binding domains and regulation of the human copper transporters ATP7B and ATP7A

TL;DR: The structure and dynamics of theMBDs are described, the current knowledge about their functional roles are reviewed, and a mechanism of regulation of ATP7B by copper‐dependent changes in the dynamics and conformation of the MBD chain is proposed.
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Direct Observation of Methylmercury and Auranofin Binding to Selenocysteine in Thioredoxin Reductase.

TL;DR: The results demonstrate for the first time the direct and complete binding of the metal atom of the inhibitors to the selenium atom in TrxR1 for both methylmercury and auranofin, indicating that TrXR1 inhibition indeed can be attributed to such direct metal-selenium binding.