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Tim Magnus

Researcher at University of Hamburg

Publications -  154
Citations -  7001

Tim Magnus is an academic researcher from University of Hamburg. The author has contributed to research in topics: Microglia & Inflammation. The author has an hindex of 38, co-authored 133 publications receiving 5338 citations. Previous affiliations of Tim Magnus include Hamburg University of Technology & Eppendorf (Germany).

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AST-120 Reduces Neuroinflammation Induced by Indoxyl Sulfate in Glial Cells.

TL;DR: It is demonstrated that sera of CKD patients induced a significant inflammation in astrocyte cells which was proportional to IS sera concentrations, and that the IS adsorbent, AST-120, reduced this inflammatory response.
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Different Roles of Mitochondria in Cell Death and Inflammation: Focusing on Mitochondrial Quality Control in Ischemic Stroke and Reperfusion.

TL;DR: In this article, the principal mitochondrial molecular mechanisms compromised during ischemic and reperfusion injury were explored, and potential neuroprotective strategies targeting mitochondrial dysfunction and mitochondrial homeostasis were delineated.
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In Vivo Blockade of Murine ARTC2.2 During Cell Preparation Preserves the Vitality and Function of Liver Tissue-Resident Memory T Cells.

TL;DR: It is concluded that in vivo blockade of ARTC2.2 during cell preparation by nanobody s+16a injection represents a valuable strategy to study the role and function of liver Trm in mice.
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Deficiency in serine protease inhibitor neuroserpin exacerbates ischemic brain injury by increased postischemic inflammation.

TL;DR: Excessive microglial activation in Ns−/− mice mediated by an increased activity of tPA results in a worse outcome further underscoring the potential detrimental proinflammatory effects of t PA.
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GPI-anchor signal sequence influences PrPC sorting, shedding and signalling, and impacts on different pathomechanistic aspects of prion disease in mice

TL;DR: The results are the first to demonstrate in vivo, that the G PI-anchor signal sequence plays a fundamental role in the GPI-anchors composition, dictating the subcellular localization of a given protein and, in the case of PrPC, influencing the development of prion disease.