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Xiu-Fen Ming

Researcher at University of Fribourg

Publications -  63
Citations -  9743

Xiu-Fen Ming is an academic researcher from University of Fribourg. The author has contributed to research in topics: Arginase & Endothelial dysfunction. The author has an hindex of 31, co-authored 59 publications receiving 8899 citations. Previous affiliations of Xiu-Fen Ming include University of Zurich & University of Basel.

Papers
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Journal ArticleDOI

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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Activation and phosphorylation of a pleckstrin homology domain containing protein kinase (RAC-PK/PKB) promoted by serum and protein phosphatase inhibitors

TL;DR: Treatment of quiescent Swiss 3T3 fibroblasts with serum, or with the phosphatase inhibitors okadaic acid and vanadate, induced a 2- to 11-fold activation of the serine/ threonine RAC protein kinase, which is a component of a signaling pathway regulated by phosphatidylinositol 3-kinase, whose action is required for RAC-PK activation by phosphorylation.
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Rho GTPase/Rho kinase negatively regulates endothelial nitric oxide synthase phosphorylation through the inhibition of protein kinase B/Akt in human endothelial cells.

TL;DR: It is demonstrated that Rho/ROCK pathway negatively regulates eNOS phosphorylation through inhibition of PKB, whereas it downregulates eNos expression independent of P KB.
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Thrombin Stimulates Human Endothelial Arginase Enzymatic Activity via RhoA/ROCK Pathway Implications for Atherosclerotic Endothelial Dysfunction

TL;DR: Higher arginase enzymatic activity is involved in atherosclerotic endothelial dysfunction in apoE−/− mice, and Targeting vascular arginases may represent a novel therapeutic possibility for atherosclerosis.
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4E-BP1 phosphorylation is mediated by the FRAP-p70s6k pathway and is independent of mitogen-activated protein kinase.

TL;DR: The data presented here demonstrate that 4E-BP1 phosphorylation is mediated by the FRAP-p70s6k pathway and is independent of mitogen-activated protein kinase.