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Nele Vanlangenakker

Researcher at Ghent University

Publications -  13
Citations -  2406

Nele Vanlangenakker is an academic researcher from Ghent University. The author has contributed to research in topics: Programmed cell death & Necroptosis. The author has an hindex of 11, co-authored 13 publications receiving 2162 citations. Previous affiliations of Nele Vanlangenakker include Flanders Institute for Biotechnology & Boston Children's Hospital.

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Necroptosis, necrosis and secondary necrosis converge on similar cellular disintegration features

TL;DR: Subcellular events during tumor necrosis factor-induced necroptosis, H2O2-induced necrosis and anti-Fas-induced secondary necrosis were studied using high-resolution time-lapse microscopy to characterize the cellular disintegration phase of the three types of necrosis.
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Many stimuli pull the necrotic trigger, an overview

TL;DR: The observation that RIPK3 ablation rescues embryonic lethality in mice deficient in caspase-8 or Fas-associated-protein-via-a-death-domain demonstrates the crucial role of this apoptotic platform in the negative control of necroptosis during development.
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Molecular Mechanisms and Pathophysiology of Necrotic Cell Death

TL;DR: This review will focus on the intracellular and intercellular signaling events in necrosis induced by different stimuli, such as oxidative stress, cytokines and pathogen-associated molecular patterns (PAMPs), which can be linked to several pathologies such as stroke, cardiac failure, neurodegenerative diseases, and infections.
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cIAP1 and TAK1 protect cells from TNF-induced necrosis by preventing RIP1/RIP3-dependent reactive oxygen species production

TL;DR: The data indicate that cIAP1 and TAK1 protect cells from TNF-induced necrosis by preventing RIP1/RIP3-dependent ROS production and enhanced RIP1 kinase activity, increased recruitment of RIP1 to Fas-associated via death domain and RIP3 (which allows necrosome formation), and elevated RIP1 Kinase-dependent accumulation of reactive oxygen species (ROS).
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TNF-induced necroptosis in L929 cells is tightly regulated by multiple TNFR1 complex I and II members.

TL;DR: It is reported here that RIP1 is a crucial mediator of canonical NF-κB activation in L929 cells, therefore questioning the relative cytoprotective contribution of RIP1 ubiquitination versus canonicalNF-κBs activation.