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Bertrand H. Rihn

Researcher at University of Lorraine

Publications -  80
Citations -  7037

Bertrand H. Rihn is an academic researcher from University of Lorraine. The author has contributed to research in topics: In vivo & Gene expression. The author has an hindex of 21, co-authored 76 publications receiving 6429 citations. Previous affiliations of Bertrand H. Rihn include Institut national de recherche et de sécurité & University of California, Berkeley.

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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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Alpha-lipoic acid in liver metabolism and disease.

TL;DR: Experimental studies and clinical trials in the last 5 years have provided new and consistent evidence for the therapeutic role of antioxidant alpha-lipoic acid in the treatment of insulin resistance and diabetic polyneuropathy, and should encourage clinicians to use alpha- Lipoic Acid in diseases affecting liver in which oxidative stress is involved.
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Microarrays as Cancer Keys: An Array of Possibilities

TL;DR: The recent developments in microarray technologies in cancer research are highlighted, the results obtained so far are focused on, and the eventual use of microarray technology for clinical applications are described.
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Selective inhibition of NF‐κB activation by the flavonoid hepatoprotector silymarin in HepG2

TL;DR: Surprisingly, tumor necrosis factor‐α‐induced NF‐κB activation was not affected by silymarin, thus demonstrating a pathway‐dependent inhibition by sallymarin.
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The human type 2 iodothyronine deiodinase is a selenoprotein highly expressed in a mesothelioma cell line.

TL;DR: Human D2 is encoded by hDio2 and is a member of the selenodeiodinase family accounting for its highly catalytic efficiency in T4 activation.