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Lars-Oliver Klotz

Researcher at University of Jena

Publications -  146
Citations -  12202

Lars-Oliver Klotz is an academic researcher from University of Jena. The author has contributed to research in topics: Peroxynitrite & Phosphorylation. The author has an hindex of 53, co-authored 138 publications receiving 11032 citations. Previous affiliations of Lars-Oliver Klotz include University of Tübingen & Ruhr University Bochum.

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Gadd153 Sensitizes Cells to Endoplasmic Reticulum Stress by Down-Regulating Bcl2 and Perturbing the Cellular Redox State

TL;DR: Gadd153 sensitizes cells to ER stress through mechanisms that involve down-regulation of Bcl2 and enhanced oxidant injury and protected cells from ER stress-induced cell death.
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Reactive Oxygen Species (Ros-Induced) Ros Release: A New Phenomenon Accompanying Induction of the Mitochondrial Permeability Transition in Cardiac Myocytes

TL;DR: A new model enabling incremental ROS accumulation in individual mitochondria in isolated cardiac myocytes via photoactivation of tetramethylrhodamine derivatives, which also served to report the mitochondrial transmembrane potential is devised, which is termed mitochondrial “ROS-induced ROS release” (RIRR).
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Redox regulation of FoxO transcription factors

TL;DR: Of particular interest are the dual role played by FoxOs in cancer development and their key role in whole body nutrient homeostasis, modulating metabolic adaptations and/or disturbances in response to low vs. high nutrient intake.
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Cellular responses to nanoparticles: Target structures and mechanisms

TL;DR: An integrated research protocol is proposed to identify fundamental cellular responses to NP in order to complement current toxicological screening strategies with a mechanism-based approach.
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Glutathione Peroxidase Protects against Peroxynitrite-mediated Oxidations A NEW FUNCTION FOR SELENOPROTEINS AS PEROXYNITRITE REDUCTASE

TL;DR: A novel function of GPx is demonstrated, and potentially of other selenoproteins containing selenocysteine or selenomethionine, in the GSH-dependent maintenance of a defense line against peroxynitrite-mediated oxidations, as a peroxlynitrite reductase.