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Huiping Zhou

Researcher at University of Tsukuba

Publications -  205
Citations -  14812

Huiping Zhou is an academic researcher from University of Tsukuba. The author has contributed to research in topics: Medicine & Unfolded protein response. The author has an hindex of 52, co-authored 169 publications receiving 12560 citations. Previous affiliations of Huiping Zhou include Veterans Health Administration & New Mexico State University.

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Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition)

Daniel J. Klionsky, +2522 more
- 21 Jan 2016 - 
TL;DR: In this paper, the authors present a set of guidelines for the selection and interpretation of methods for use by investigators who aim to examine macro-autophagy and related processes, as well as for reviewers who need to provide realistic and reasonable critiques of papers that are focused on these processes.
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Bile acids as regulatory molecules.

TL;DR: Current knowledge of how bile acids regulate hepatic lipid and glucose metabolism through the activation of specific nuclear receptors and cell signaling pathways is summarized.
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The plasma lipidomic signature of nonalcoholic steatohepatitis.

TL;DR: Although increased lipogenesis, desaturases, and LOX activities characterize NAFL and NASH, impaired peroxisomal polyunsaturated fatty acid (PUFA) metabolism and nonenzymatic oxidation is associated with progression to NASH.
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Increased Hepatic Synthesis and Dysregulation of Cholesterol Metabolism Is Associated with the Severity of Nonalcoholic Fatty Liver Disease

TL;DR: Dysregulated cholesterol metabolism in NAFLD is demonstrated which may contribute to disease severity and cardiovascular risks and is associated with increased SREBP-2 maturation, HMG CoA reductase (HMGCR) expression and decreased phosphorylation of HMGCR.
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Prostaglandin catabolizing enzymes.

TL;DR: The primary catabolic pathway of prostaglandins and related eicosanoids is initiated by the oxidation of 15(S)-hydroxyl group catalyzed by NAD+-dependent 15-hydroxyprostaglandin dehydrogenase (15-PGDH) followed by the reduction of delta13 double bond catalyzing by NADPH/NADH dependent delta13-15-ketoprostagland in reductase (13-PGR).