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Marla J. Berry

Researcher at University of Hawaii at Manoa

Publications -  145
Citations -  12166

Marla J. Berry is an academic researcher from University of Hawaii at Manoa. The author has contributed to research in topics: Selenoprotein & Selenocysteine. The author has an hindex of 52, co-authored 140 publications receiving 11062 citations. Previous affiliations of Marla J. Berry include University of Hawaii & Harvard University.

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Podocyte specific knock out of selenoproteins does not enhance nephropathy in streptozotocin diabetic C57BL/6 mice

TL;DR: Loss of podocyte selenoproteins in streptozotocin diabetic C57BL/6 mice does not lead to increased oxidative stress as assessed by nitrotyrosine and NAD(P)H dehydrogenase, quinone 1 immunostaining, nor does it lead to worsening nephropathy.
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The Inhibitory Effect of Bamboo Extract on the Development of 7,12-Dimethylbenz[a]anthracene (DMBA)-induced Breast Cancer

TL;DR: The results indicate that BEX possesses a potent anti‐breast cancer effect, and the upregulation of SULT activity, therefore estrogen metabolism may be the underlying mechanism.
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Selenophosphate synthetase 2 is essential for selenoprotein biosynthesis

TL;DR: In this paper, the roles of SPS2 and SPS1 in selenoprotein synthesis in vivo were investigated and it was shown that SPS 2 was essential for generating the selenium donor for selenocysteine biosynthesis in mammals.
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Relationship between selenoprotein P and selenocysteine lyase: Insights into selenium metabolism.

TL;DR: A potential interplay between SelenoP and Scly is evaluated, providing further insights into the regulation of selenium metabolism and regulated by Se levels in a cell type‐specific manner in vitro and in vivo.
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Glutathione depletion in hippocampal cells increases levels of H and L ferritin and glutathione S-transferase mRNAs.

TL;DR: Investigation of changes in mRNA profile in HT22 hippocampal cells following administration of homocysteic acid (HCA) increases the levels of the mRNAs encoding at least three proteins involved in protection from oxidant injury, the m RNAs encoding heavy (H) and light (L) ferritin and glutathione S‐transferase (GST).